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References
Rahimtula, A.D. and P.J. O’Brien (1977). The peroxidase nature of cytochrome P450. In V. Ullrich, I. Roots, A. Hildebrandt, R.W. Estabrook, and A.H. Conney (eds.), Microsomes and Drug Oxidations, Pergamon Press, Elmsford, NY, pp. 210–217.
Rodrigues, A.D., D. Fernandez, M.A. Nosarzewski, W.M. Pierce, and R.A. Prough (1991). Inhibition of hepatic microsomal cytochrome P-450 dependent monooxygenation activity by the antioxidant 3-tert-butyl-4-hydroxyanisole. Chem. Res. Toxicol. 4, 281–289.
Kharasch, E.D., N.K. Wendel, and R.F. Novak (1987). Anthracenedione antineoplastic agent effects on drug metabolism in vitro and in vivo: Relationship between structure and mechanism of inhibition. Fundam. Appl. Toxicol. 9, 18–25.
Testa, B. and P. Jenner (1981). Inhibitors of cytochrome P-450s and their mechanism of action. Drug. Metab. Rev. 12, 1–117.
Correia, M.A., and P.R. Ortiz de Montellano (1993). Inhibitors of cytochrome P450 and possibilities for their therapeutic application. In K. Ruckpaul (ed.), Frontiers in Biotransformation. Akademie-Verlag, Berlin, pp. 74–146.
Murray, M. and G.F. Reidy (1990). Selectivity in the inhibition of mammalian cytochromes P-450 by chemical agents. Pharmacol. Rev. 42, 85–101.
Ortiz de Montellano, P.R. (1988). Suicide substrates for drug metabolizing enzymes: Mechanism and biological consequences. In G.G. Gibson (ed.), Progress in Drug Metabolism. Taylor and Francis, New York, pp. 99–148.
Vanden Bossche, H. (1992). Inhibitors of P450-dependent steroid biosynthesis: From research to medical treatment. J. Steroid Biochem. Mol. Biol. 43, 1003–1021.
Rendic, S. and F.J. Di Carlo (1997). Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors. Drug Metab. Rev. 29, 413–580.
Lewis, D.F. (2003). Human cytochromes P450 associated with the Phase 1 metabolism of drugs and other xenobiotics: A compilation of substrates and inhibitors of the CYP1, CYP2 and CYP3 families. Curr. Med. Chem. 10, 1955–1972.
Kent, U.M., M.I. Juschyshyn, and P.F. Hollenberg (2001). Mechanism-based inactivators as probes of cytochrome P450 structure and function. Curr. Drug Metab. 2, 215–243.
Brueggemeier, R.W. (2002). Aromatase inhibitors in breast cancer therapy. Expert Rev. Anticancer Ther. 2, 181–191.
Sato, A. and T. Nakajima (1979). Dose-dependent metabolic interaction between benzene and toluene in vivo and in vitro. Toxicol. Appl. Pharmacol. 48, 249–256.
Watkins, P.B. (1990). Role of cytochromes P450 in drug metabolism and hepatotoxicity. Semin. Liver Dis. 10, 235–250.
Jefcoate, C.R. (1978). Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Meth. Enzymol. 52, 258–279.
Kumaki, K., M. Sato, H. Kon, and D.W. Nebert (1978). Correlation of type I, type II, and reverse type I difference spectra with absolute changes in spin state of hepatic microsomal cytochrome P-450 iron from five mammalian species. J. Biol. Chem. 253, 1048–1058.
Schenkman, J.B., S.G. Sligar, and D.L. Cinti (1981). Substrate interactions with cytochrome P-450. Pharmacol. Ther. 12, 43–71.
Sligar, S.G., D.L. Cinti, G.G. Gibson, and J.B. Schenkman (1979). Spin state control of the hepatic cytochrome P-450 redox potential. Biochem. Biophys. Res. Commun. 90, 925–932.
Guengerich, F. P. (1983). Oxidation-reduction properties of rat liver cytochromes P450 and NADPH-cytochrome P-450 reductase related to catalysis in reconstituted systems. Biochemistry 22, 2811–2820.
Kitada, M., K. Chiba, T. Kamataki. and H. Kitagawa (1977). Inhibition by cyanide of drug oxidations in rat liver microsomes. Jpn. J. Pharmacol. 27, 601–608.
Ho, B. and N. Castagnoli (1980). Trapping of metabolically generated electrophilic species with cyanide ion: Metabolism of 1-benzylpyrrolidine. J. Med. Chem. 23, 133–139.
Sono, M. and J.H. Dawson (1982). Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands: Spin state and ligand affinity comparison to myoglobin. J. Biol. Chem. 257, 5496–5502.
Backes, W.L., M. Hogaboom, and W.J. Canady (1982). The true hydrophobicity of microsomal cytochrome P-450 in the rat: Size dependence of the free energy of binding of a series of hydrocarbon substrates from the aqueous phase to the enzyme and to the membrane as derived from spectral binding data. J. Biol. Chem. 257, 4063–4070.
Wink, D.A., Y. Osawa, J.F. Darbyshe, C.R. Jones, S.C. Eshenaur, and R.W. Nims (1993). Inhibition of cytochromes P450 by nitric oxide and a nitric oxide-releasing agent. Arch. Biochem. Biophys. 300, 115–123.
Khatsenko, O.G., S.S. Gross, A.B. Rifkind, and J.R. Vane (1993). Nitric oxide is a mediator of the decrease in cytochrome P450-dependent metabolism caused by immunostimulants. Proc. Natl. Acad. Sci. USA 90, 11147–11151.
Kim, Y.-M., H.A. Bergonia, C. Müller, B.R. Pitt, W.D. Watkins, and J.R. Lancaster, Jr. (1995). Loss and degradation of enzyme-bound heme induced by cellular nitric oxide synthesis. J. Biol. Chem. 270, 5710–5713.
Alonso-Galicia, M., H. Drummond, K. Reddy, J. Falck, and R. Roman (1997). Inhibition of 20-HETE production contributes to the vascular responses to nitric oxide. Hypertension 29, 320–325.
Drewett, J.G., R.L. Adams-Hays, B.Y. Ho, and D.J. Hegge (2002). Nitric oxide potently inhibits the rate-limiting enzymatic step in steroidogenesis. Mol. Cell. Endocrinol. 194, 39–50.
Hanson, L.K., W.A. Eaton, S.G. Sligar, I.C. Gunsalus, M. Gouterman, and C.R. Connell (1976). Origin of the anomalous Soret spectra of carboxycytochrome P450. J. Am. Chem. Soc. 98, 2672–2674.
Omura, T. and R. Sato (1964). The carbon monoxide-binding pigment of liver microsomes. 1. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370–2378.
Collman, J.P. and T.N. Sorrell (1975). A model for the carbonyl adduct of ferrous cytochrome P-450. J. Am. Chem. Soc. 97, 4133–4134.
Leeman, T., P. Bonnabry, and P. Dayer (1994). Selective inhibition of major drug metabolizing cytochrome P450 isozymes in human liver microsomes by carbon monoxide. Life Sci. 54, 951–956.
Canick, J.A. and K.J. Ryan (1976). Cytochrome P-450 and the aromatization of 16-alpha-hydroxy-testosterone and androstenedione by human placental microsomes. Mol. Cell. Endocrinol. 6, 105–115.
Gibbons, G.F., C.R. Pullinger, and K.A. Mitropoulos (1979). Studies on the mechanism of lanosterol 14-alpha-demethylation: A requirement for two distinct types of mixed-function-oxidase systems. Biochem. J. 183, 309–315.
Hansson, R. and K. Wikvall (1982). Hydroxylations in biosynthesis of bile acids: Cytochrome P-450 LM4 and 12α-hydroxylation of 5β-cholestane-3α,7α-diol. Eur. J. Biochem. 125, 423–429.
Meigs, R.A. and K.J. Ryan (1971). Enzymatic aromatization of steroids. I. Effects of oxygen and carbon monoxide on the intermediate steps of estrogen biosynthesis. J. Biol. Chem. 246, 83–87.
Zachariah, P.K. and M.R. Juchau (1975). Interactions of steroids with human placental cytochrome P-450 in the presence of carbon monoxide. Life Sci. 16, 1689–1692.
Tuckey, R.C. and H. Kamin (1983). Kinetics of O2 and CO binding to adrenal cytochrome P-450scc: Effect of cholesterol, intermediates, and phosphatidylcholine vesicles. J. Biol. Chem. 258, 4232–4237.
Cohen, G.M. and G.J. Mannering (1972). Involvement of a hydrophobic site in the inhibition of the microsomal para-hydroxylation of aniline by alcohols. Mol. Pharmacol. 8, 383–397.
Gerber, M.C., G.A Tejwani, N. Gerber, and J.R. Bianchine (1985). Drug interactions with cimetidine: An update. Pharmacol. Ther. 27, 353–370.
Testa, B. (1981). Structural and electronic factors influencing the inhibition of aniline hydroxylation by alcohols and their binding to cytochrome P-450. Chem. Biol. Interact. 34, 287–300.
Wattenberg, L.W., L.K.T. Lam, and A.V. Fladmoe, (1979). Inhibition of chemical carcinogen-induced neoplasia by coumarins and alpha-angelicalactone. Cancer Res. 39, 1651–1654.
Remmer, H., J. Schenkman, R.W. Estabrook, H. Sasame, J. Gillette, S. Narasimhulu et al. (1966). Drug interaction with hepatic microsomal cytochrome. Mol. Pharmacol. 2, 187–190.
Jefcoate, C.R., J.L. Gaylor, and R.L. Callabrese (1969). Ligand interactions with cytochrome P-450. 1. Binding of primary amines. Biochemistry 8, 3455–3463.
Schenkman, J.B., H Remmer, and R.W. Estabrook (1967). Spectral studies of drug interaction with hepatic microsomal cytochrome P-450. Mol. Pharmacol. 3, 113–123.
Dominguez, O.V. and L.T. Samuels (1963). Mechanism of inhibition of adrenal steroid 11-betahydroxylase by methopyrapone (metopirone). Endocrinology 73, 304–309.
Temple, T.E. and G.W. Liddle (1970). Inhibitors of adrenal steroid biosynthesis. Ann. Rev. Pharmacol. 10, 199–218.
Rogerson, T.D., C.F. Wilkinson, and K. Hetarski (1977). Steric factors in the inhibitory interaction of imidazoles with microsomal enzymes. Biochem. Pharmacol. 26, 1039–1042.
Wilkinson, C.F., K Hetarski, G.P. Cantwell, and F.J. DiCarlo (1974). Structure-activity relationships in the effects of 1-alkylimidazoles on microsomal oxidation in vitro and in vivo. Biochem. Pharmacol. 23, 2377–2386.
Duquette, P.H., R.R. Erickson, and J.L. Holtzman (1983). Role of substrate lipophilicity on the N-demethylation and type I binding of 3-O-alkylmorphine analogues. J. Med. Chem. 26, 1343–1348.
Smith, S.R. and M.J. Kendall (1988). Ranitidine versus cimetidine. A comparison of their potential to cause clinically important drug interactions. Clin. Pharmacokinet. 15, 44–56.
Ator, M.A. and Ortiz P.R. de Montellano (1990). Mechanism-based (suicide) enzyme inactivation. In D.S. Sigman and P.D. Boyer (eds.), The Enzymes: Mechanisms of Catalysis, Vol. 19, 3rd edn., Academic Press, New York, pp. 214–282.
Silverman, R.B. (1988). Mechanism-Based Enzyme Inactivation: Chemistry and Enzymology. CRC Press, Boca Raton, FL.
Dalvi, R.R. (1987). Cytochrome P-450-dependent covalent binding of carbon disulfide to rat liver microsomal protein in vitro and its prevention by reduced glutathione. Arch. Toxicol. 61, 155–157.
De Matteis, F.A. and A.A. Seawright (1973). Oxidative metabolism of carbon disulphide by the rat: Effect of treatments which modify the liver toxicity of carbon disulphide. Chem. Biol. Interact. 7, 375–388.
Bond, E.J. and F.A. De Matteis (1969). Biochemical changes in rat liver after administration of carbon disulphide, with particular reference to microsomal changes. Biochem. Pharmacol. 18, 2531–2549.
Halpert, J., D. Hammond, and R.A. Neal (1980). Inactivation of purified rat liver cytochrome P-450 during the metabolism of parathion (diethyl p-nitrophenyl phosphorothionate). J. Biol. Chem. 255, 1080–1089.
Neal, R.A., T Kamataki, M. Lin, K.A. Ptashne, R. Dalvi, and R.Y. Poore (1977). Studies of the formation of reactive intermediates of parathion. In D.J. Jollow, J.J. Koesis, R. Snyder, and H. Vaino (eds.), Biological Reactive Intermediates. Plenum Press, New York, pp. 320–332.
Miller, G.E., M.A. Zemaitis, and F.E. Greene (1983). Mechanisms of diethyldithiocarbamateinduced loss of cytochrome P-450 from rat liver. Biochem. Pharmacol. 32, 2433–2442.
El-hawari, A.M. and G.L. Plaa (1979). Impairment of hepatic mixed-function oxidase activity by alpha-and beta-naphthylisothiocyanate: Relationship to hepatotoxicity. Toxicol. Appl. Pharmacol. 48, 445–458.
Lee, P.W., T Arnau, and R.A. Neal (1980). Metabolism of alpha-naphthylthiourea by rat liver and rat lung microsomes. Toxicol. Appl. Pharmacol. 53, 164–173.
Lopez-Garcia, M.P., P.M. Dansette, and D. Mansuy (1993). Thiophene derivatives as new mechanism-based inhibitors of cytochromes P450: Inactivation of yeast-expressed human liver P450 2C9 by tienilic acid. Biochemistry 33, 166–175.
Lopez-Garcia, M.P., P.M. Dansette, P. Valadon, C. Amar, P.H. Beaune, F.P. Guengerich et al. (1993). Human liver P450s expressed in yeast as tools for reactive metabolite formation studies: Oxidative activation of tienilic acid by P450 2C9 and P450 2C10. Eur. J. Biochem. 213, 223–232.
Menard, R.H., T.M Guenthner, A.M. Taburet, H. Kon, L.R. Pohl, J.R. Gillette et al. (1979). Specificity of the in vitro destruction of adrenal and hepatic microsomal steroid hydroxylases by thiosterols. Mol. Pharmacol. 16, 997–1010.
Kossor, D.C., S Kominami, S. Takemori, and H.D. Colby (1991). Role of the steroid 17α-hydroxylase in spironolactone-mediated destruction of adrenal cytochrome P-450. Mol. Pharmacol. 40, 321–325.
Decker, C., K. Sugiyama, M. Underwood, and M.A. Correia (1986). Inactivation of rat hepatic cytochrome P-450 by spironolactone. Biochem. Biophys. Res. Commun. 136, 1162–1169.
Decker, C.J., M.S. Rashed, T.A. Baillie, D. Maltby, and M.A. Correia (1989). Oxidative metabolism of spironolactone: Evidence for the involvement of electrophilic thiosteroid species in drug-mediated destruction of rat hepatic cytochrome P450. Biochemistry 28, 5128–5136.
Menard, R.H., T.M. Guenthner, H. Kon, and J.R. Gillette (1979). Studies on the destruction of adrenal and testicular cytochrome P-450 by spironolactone: Requirement for the 7-alpha-thio group and evidence for the loss of the heme and apoproteins of cytochrome P-450. J. Biol. Chem. 254, 1726–1733.
Sherry, J.H., J.P. O’Donnell, L. Flowers, L.B. Lacagnin, and H.D. Colby (1986). Metabolism of spironolactone by adrenocortical and hepatic microsomes: Relationship to cytochrome P-450 destruction. J. Pharmacol. Exp. Ther. 236, 675–680.
Colby, H.D., J.P. O’Donnell, N. Lynn, D.C. Kossor, P.B. Johnson, and M. Levitt (1991). Relationship between covalent binding to microsomal protein and the destruction of adrenal cytochrome P-450 by spironolactone. Toxicology 67, 143–154.
Decker, C.J., J.R. Cashman, K. Sugiyama, D. Maltby, and M.A. Correia (1991). Formation of glutathionyl-spironolactone disulfide by rat liver cytochromes P450 or hog live flavin-containing monooxygenases: A functional probe of two-electron oxidations of the thiosteroid? Chem. Res. Toxicol. 4, 669–677.
Halpert, J. and R.A. Neal (1980). Inactivation of purified rat liver cytochrome P-450 by chloramphenicol. Mol. Pharmacol. 17, 427–434.
Halpert, J. (1982). Further studies of the suicide inactivation of purified rat liver cytochrome P-450 by chloramphenicol. Mol. Pharmacol. 21, 166–172.
Halpert, J. (1981). Covalent modification of lysine during the suicide inactivation of rat liver cytochrome P-450 by chloramphenicol. Biochem. Pharmacol. 30, 875–881.
Halpert, J., B. Naslund, and I. Betner (1983). Suicide inactivation of rat liver cytochrome P-450 by chloramphenicol in vivo and in vitro. Mol. Pharmacol. 23, 445–452.
Halpert, J., C. Balfour, N.E. Miller, and L.S. Kaminsky (1986). Dichloromethyl compounds as mechanism-based inactivators of rat liver cytochromes P450 in vitro. Mol. Pharmacol. 30, 19–24.
Halpert, J., J.-Y. Jaw, C. Balfour, and L.S. Kaminsky (1990). Selective inactivation by chlorofluoroacetamides of the major phenobarbital-inducible form(s) of rat liver cytochrome P-450. Drug Metab. Dispos. 18, 168–174.
CaJacob, C.A., W. Chan, E. Shephard, and P.R. Ortiz de Montellano (1988). The catalytic site of rat hepatic lauric acid ω-hydroxylase. Protein vs prosthetic heme alkylation in the ω-hydroxylation of acetylenic fatty acids. J. Biol. Chem. 263, 18640–18649.
Hammons, G.J., W.L. Alworth, N.E. Hopkins, F.P. Guengerich, and F.F. Kadlubar (1989). 2-Ethynylnaphthalene as a mechanism-based inactivator of the cytochrome P-450-catalyzed N-oxidation of 2-naphthylamine. Chem. Res. Toxicol. 2, 367–374.
Yun, C.-H., M.V. Martin, N.E. Hopkins, W.L. Alworth, G.J. Hammons, and F.P. Guengerich (1992). Modification of cytochrome P4501A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene. Biochemistry 31, 10556–10563.
Gan, L.-S.L., A.L. Acebo, and W.L. Alworth (1984). 1-Ethynylpyrene, a suicide inhibitor of cytochrome P-450 dependent benzo(a)pyrene hydroxylase activity in liver microsomes. Biochemistry 23, 3827–3836.
Roberts, E.S., N.E. Hopkins, W.L. Alworth, and P.F. Hollenberg (1993). Mechanism-based inactivation of cytochrome P450 2B1 by 2-ethynylnaphthalene: Identification of an active-site peptide. Chem. Res. Toxicol. 6, 470–479.
Chan, W.K., Z Sui, and P.R. Ortiz de Montellano (1993). Determinants of protein modification versus heme alkylation: Inactivation of cytochrome P450 1A1 by 1-ethynylpyrene and phenylacetylene. Chem. Res. Toxicol. 6, 38–45.
Helvig, C., C. Alayrac, C. Mioskowski, D. Koop, D. Poullain, F. Durst et al. (1997). Suicide inactivation of cytochrome P450 by midchain and terminal acetylenes. A mechanistic study of inactivation of a plant lauric acid omega-hydroxylase. J. Biol. Chem. 272, 414–421.
Halpert, J., J.-Y. Jaw, and C. Balfour (1989). Specific inactivation by 17β-substituted steroids of rabbit and rat liver cytochromes P-450 responsible for progesterone 21-hydroxylation. Mol. Pharmacol. 34, 148–156.
Stevens, J.C., J-Y. Jaw, C.-T. Peng, and J. Halpert (1991). Mechanism-based inactivation of bovine adrenal cytochromes P450 C-21 and P450 17α by 17β-substituted steroids. Biochemistry 30, 3649–3658.
Guengerich, F.P. (1988). Oxidation of 17 alphaethynylestradiol by human liver cytochrome P-450. Mol. Pharmacol. 33, 500–508.
Guengerich, F.P. (1990). Metabolism of 17 alphaethynylestradiol in humans. Life Sc. 47, 1981–1988.
Guengerich, F.P. (1990). Inhibition of oral contraceptive steroid-metabolizing enzymes by steroids and drugs. Am. J. Obstet. Gynecol. 163 (Pt 2), 2159–2163.
Lin, H.L., U.M. Kent, and P.F. Hollenberg, (2002). Mechanism-based inactivation of cytochrome P450 3A4 by 17 alpha-ethynylestradiol: Evidence for heme destruction and covalent binding to protein. J. Pharmacol. Exp. Ther. 301, 160–167.
Kent, U.M., D.E. Mills, R.V. Rajnarayanan, W.L. Alworth, and P.F. Hollenberg, (2002). Effect of 17-α-ethynylestradiol on activities of cytochrome P450 2B (P450 2B) enzymes: Characterization of inactivation of P450s 2B1 and 2B6 and identification of metabolites. J. Pharmacol. Exp. Ther. 300, 549–558.
Guengerich, F.P. (1990). Mechanism-based inactivation of human liver microsomal cytochrome P-450 IIIA4 by gestodene. Chem. Res. Toxicol. 3, 363–371.
Roberts, E.S., N.E. Hopkins, E.J. Zalulec, D.A. Gage, W.L. Alworth, and P.F. Hollenberg (1994). Identification of active-site peptides from 3H-labeled 2-ethynylnaphthalene-inactivated P450 2B1 and 2B4 using amino acid sequencing and mass spectrometry. Biochemistry 33, 3766–3771.
Regal, K.A., M.L. Schrag, L.C. Wienkers, U.M. Kent, and P.F. Hollenberg (2000). Mechanism-based inactivation of cytochrome P450 2B1 by 7-ethynylcoumarin: Verification of apo-P450 adduction by electrospray ion trap mass spectrometry. Chem. Res. Toxicol. 13, 262–270.
He, K., T.F. Woolf, and P.F. Hollenberg (1999). Mechanism-based inactivation of cytochrome P-450-3A4 by mifepristone (RU486). J. Pharmacol. Exp. Ther. 288, 791–797.
Khan, K.K., Y.Q. He, M.A. Correia, and J.R. Halpert (2002). Differential oxidation of mifepristone by cytochromes P450 3A4 and 3A5: Selective inactivation of P450 3A4. Drug Metab. Dispos. 30, 985–990.
Lunetta, J.M., K. Sugiyama, and M.A. Correia (1989). Secobarbital-mediated inactivation of rat liver cytochrome P-450b: A mechanistic reappraisal. Mol. Pharmacol. 35, 10–17.
Letteron, P., V. Descatoire, D. Larrey, M. Tinel, J. Geneve, and D. Pessayre (1986). Inactivation and induction of cytochrome P-450 by various psoralen derivatives in rats. J. Pharmacol. Exp. Ther. 238, 685–692.
Fouin-Fortunet, H., M. Tinel, V. Descatoire, P. Letteron, D. Larrey, J. Geneve et al. (1986). Inactivation of cytochrome P450 by the drug methoxsalen. J. Pharmacol. Exp. Ther. 236, 237–247.
Tinel, M., J. Belghiti, V. Descatoire, G. Amouyal, P. Letteron, J. Geneve (1987). Inactivation of human liver cytochrome P-450 by the drug methoxsalen and other psoralen derivatives. Biochem. Pharmacol. 36, 951–955.
Labbe, G., V. Descatoire, P. Beaune, P. Letteron, D. Larrey, and D. Pessayre (1989). Suicide inactivation of cytochrome P450 by methoxsalen. Evidence for the covalent binding of a reactive intermediate to the protein moiety. J. Pharmacol. Exp. Ther. 250, 1034–1042.
Mays, D.C., J.B. Hilliard, D.D. Wong, M.A. Chambers, S.S. Park, H.V. Gelboin et al. (1990). Bioactivation of 8-methoxypsoralen and irreversible inactivation of cytochrome P450 in mouse liver microsomes: Modification by monoclonal antibodies, inhibition of drug metabolism and distribution of covalent adducts. J. Pharmacol. Exp. Ther. 254, 720–731.
Khojasteh-Bakht, S.C., L.L. Koenigs, R.M. Peter, W.F. Trager, and S.D. Nelson (1998). (R)-(+)-Menthofuran is a potent, mechanism-based inactivator of human liver cytochrome P450 2A6. Drug Metab. Dispos. 26, 701–704.
Cai, Y., D. Bennett, R.V. Nair, O. Ceska, M.J. Ashwood-Smith, and J. DiGiovanni (1993). Inhibition and inactivation of murine hepatic ethoxy-and pentoxyresorufin O-dealkylase by naturally occurring coumarins. Chem. Res. Toxicol. 6, 872–879.
Cai, Y., W. Baer-Dubowska, M.J. Ashwood-Smith, O. Ceska, S. Tachibana, and J. DiGiovanni (1996). Mechanism-based inactivation of hepatic ethoxyresorufin O-dealkylation activity by naturally occurring coumarins. Chem. Res. Toxicol. 9, 729–736.
Koenigs, L.L., and W.F. Trager (1998). Mechanism-based inactivation of P450 2A6 by furanocoumarins. Biochemistry 37, 10047–10061.
Schmiedlin-Ren, P., D.J. Edwards, M.E. Fitzsimmons, K. He, K.S. Lown, P.M. Woster et al. (1997). Mechanisms of enhanced oral availability of CYP3A4 substrates by grapefruit constituents. Decreased enterocyte CYP3A4 concentration and mechanism-based inactivation by furanocoumarins. Drug Metab. Dispos. 25, 1228–1233.
Lown, K.S., D.G. Bailey, R.J. Fontana, S.K. Janardan, C.H. Adair, L.A. Fortlage et al. (1997). Grapefruit juice increases felodipine oral availability in humans by decreasing intestinal CYP3A protein expression. J. Clin. Invest. 99, 2545–2553.
He, K., K.R. Iyer, R.N. Hayes, M.W. Sinz, T.F. Woolf, and P.F. Hollenberg (1998). Inactivation of cytochrome P450 3A4 by bergamottin, a component of grapefruit juice, Chem. Res. Toxicol. 11, 252–259.
Chiba, M., J.A. Nishime, and J.H. Lin (1995). Potent and selective inactivation of human liver microsomal cytochrome P-450 isoforms by L-754, 394, an investigational human immune deficiency virus protease inhibitor. J. Pharmacol. Exp. Ther. 275, 1527–1534.
Sahali-Sahly, Y., S.K. Balani, J.H. Lin, and T.A. Baillie (1996). In vitro studies on the metabolic activation of the furanopyridine L-754,394, a highly potent and selective mechanism-based inhibitor of cytochrome P450 3A4. Chem. Res. Toxicol. 9, 1007–1012.
Lightning, L.K., J.P. Jones, T. Friedberg, M.P. Pritchard, M. Shou, T.H. Rushmore et al. (2000). Mechanism-based inactivation of cytochrome P450 3A4 by L-754,394. Biochemistry 39, 4276–4287.
Masubuchi, Y., T. Nakano, A. Ose, and T. Horie (2001). Differential selectivity in carbamazepine-induced inactivation of cytochrome P450 enzymes in rat and human liver. Arch. Toxicol. 75, 538–543.
Mani, C., R. Pearce, A. Parkinson, and D. Kupfer (1994). Involvement of cytochrome P4503A in catalysis of tamoxifen activation and covalent binding to rat and human liver microsomes. Carcinogenesis 15, 2715–2720.
Sridar, C., U.M. Kent, L.M. Notley, E.M. Gillam, and P.F. Hollenberg (2002). Effect of tamoxifen on the enzymatic activity of human cytochrome CYP2B6, J. Pharmacol. Exp. Ther. 301, 945–952.
Zhao, X.J., D.R. Jones, Y.H. Wang, S.W. Grimm, and S.D. Hall (2002). Reversible and irreversible inhibition of CYP3A enzymes by tamoxifen and metabolites. Xenobiotica 32, 863–878.
Liu, H., M. Santostefano, and S. Safe (1994). 2-Phenylphenanthridinone and related compounds: Aryl hydrocarbon receptor agonists and suicide inactivators of P4501A1. Arch. Biochem. Biophys. 313, 206–214.
Butler, A.M. and M. Murray (1993). Inhibition and inactivation of constitutive cytochromes P450 in rat liver by parathion, Mol. Pharmacol. 43, 902–908.
Murray, M. and A.M. Butler (1995). Identification of a reversible component in the in vitro inhibition of rat hepatic cytochrome P450 2B1 by parathion. J. Pharmacol. Exp. Ther. 272, 639–644.
Butler, A.M. and M. Murray (1997). Biotransformation of parathion in human liver: Participation of CYP3A4 and its inactivation during microsomal parathion oxidation. J. Pharmacol. Exp. Ther. 280, 966–973.
Murray, M. and A.M. Butler (1994). Hepatic biotransformation of parathion: Role of cytochrome P450 in NADPH-and NADH-mediated microsomal oxidation in vitro. Chem. Res. Toxicol. 7, 792–799.
Chambers, J.E. and H.W. Chambers (1990). Time course of inhibition of acetylcholinesterase and aliesterases following parathion and paraoxon exposures in rats. Toxicol. Appl. Pharmacol. 103, 420–429.
Koenigs, L.L., R.M. Peter, A.P. Hunter, R.L. Haining, A.E. Rettie, T. Friedberg et al. (1999). Electrospray ionization mass spectrometric analysis of intact cytochrome P450: Identification of tienilic acid adducts to P450 2C9. Biochemistry 38, 2312–2319.
Ha-Duong, N.T., S. Dijols, A.C. Macherey, J.A. Goldstein, P.M. Dansette, and D. Mansuy (2001). Ticlopidine as a selective mechanism-based inhibitor of human cytochrome P450 2C19. Biochemistry 40, 12112–12122.
Donahue, S.R., D.A. Flockhart, D.R. Abernethy, and J.W. Ko (1997). Ticlopidine inhibition of phenytoin metabolism mediated by potent inhibition of CYP2C19. Clin. Pharmacol. Ther. 62, 572–577.
Klaassen, S.L. (1998). Ticlopidine-induced phenytoin toxicity. Ann. Pharmacother. 32, 1295–1298.
Lopez-Ariztegui, N., M. Ochoa, M.J. Sanchez-Migallon, C. Nevado, and M. Martin (1998). Acute phenytoin poisoning secondary to an interaction with ticlopidine. Rev. Neurol. 26, 1017–1018.
Donahue, S., D.A. Flockhart, and D.R. Abernethy (1999). Ticlopidine inhibits phenytoin clearance. Clin. Pharmacol. Ther. 66, 563–568.
Richter, T., K. Klein, T.E. Murdter, M. Eichelbaum, M. Schwab, and U.M. Zanger (2003). Clopidogrel and ticlopidine are specific mechanism-based inhibitors of human cytochrome P450 2B6. Proceedings of the 13th International Conference on Cytochromes P450, Prague, Czech Republic, p. S119.
Saunders, F. J. and R.L. Alberti (1978). Aldactone: Spironolactone: A Comprehensive Review. Searle, New York.
Kassahun, K., P.G. Pearson, W. Tang, I. McIntosh, K. Leung, C. Elmore et al. (2001). Studies on the metabolism of troglitazone to reactive intermediates in vitro and in vivo. Evidence for novel biotransformation pathways involving quinone methide formation and thiazolidinedione ring scission. Chem. Res. Toxicol. 14, 62–70.
Gitlin, N., N.L. Julie, C.L. Spurr, K.M. Lim, and H.M. Juarbe (1998). Two cases of severe clinical and histologic hepatotoxicity associated with troglitazone. Ann. Intern. Med. 129, 36–38.
Neuschwander-Tetri, B.A., W.L. Isley, J.C. Oki, S. Ramrakhiani, S.G. Quiason, N.J. Phillips et al. (1998). Troglitazone-induced hepatic failure leading to liver transplantation. A case report. Ann. Intern. Med. 129, 38–41.
Chen, Q., J.S. Ngui, G.A. Doss, R.W. Wang, X. Cai, F.P. DiNinno et al. (2002). Cytochrome P450 3A4-mediated bioactivation of raloxifene: Irreversible enzyme inhibition and thiol adduct formation. Chem. Res. Toxicol. 15, 907–914.
Kempf, D.J., K.C. Marsh, J.F. Denissen, E. McDonald, S. Vasavanonda, C.A. Flentge et al. (1995). ABT-538 is a potent inhibitor of human immunodeficiency virus protease and has high oral bioavailability in humans. Proc. Natl. Acad. Sci. USA 92, 2484–2488.
Kempf, D.J., K.C. Marsh, G. Kumar, A.D. Rodrigues, J.F. Denissen, E. McDonald et al. (1997). Pharmacokinetic enhancement of inhibitors of the human immunodeficiency virus protease by coadministration with ritonavir. Antimicrob. Agents Chemother. 41, 654–660.
Koudriakova, T., E. Latsimirskaia, I. Utkin, E. Gangl, P. Vouros, E. Storozhuk et al. (1998). Metabolism of the human immunodeficiency virus protease inhibitors indinavir and ritonavir by human intestinal microsomes and expressed cytochrome P4503A4/3A5: Mechanism-based inactivation of cytochrome P4503A by ritonavir. Drug Metab. Dispos. 26, 552–561.
Smith, T.J., Z. Guo, C. Li, S.M. Ning, P.E. Thomas, and C.S. Yang (1993). Mechanisms of inhibition of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone bioactivation in mouse by dietary phenethyl isothiocyanate. Cancer Res. 53, 3276–3282.
Moreno, R.L., T. Goosen, U.M. Kent, F.L. Chung, and P.F. Hollenberg (2001). Differential effects of naturally occurring isothiocyanates on the activities of cytochrome P450 2E1 and the mutant P450 2E1 T303A. Arch. Biochem. Biophys. 391, 99–110.
Nakajima, M., R. Yoshida, N. Shimada, H. Yamazaki, and T. Yokoi (2001). Inhibition and inactivation of human cytochrome P450 isoforms by phenethyl isothiocyanate. Drug Metab. Dispos. 29, 1110–1113.
Goosen, T.C., U.M. Kent, L. Brand, and P.F. Hollenberg (2000). Inactivation of cytochrome P450 2B1 by benzyl isothiocyanate, a chemopreventative agent from cruciferous vegetables. Chem. Res. Toxicol. 13, 1349–1359.
Goosen, T.C., D.E. Mills, and P.F. Hollenberg (2001). Effects of benzyl isothiocyanate on rat and human cytochromes P450: Identification of metabolites formed by P450 2B1. J. Pharmacol. Exp. Ther. 296, 198–206.
Moreno, R.L., U.M. Kent, K. Hodge, and P.F. Hollenberg (1999). Inactivation of cytochrome P450 2E1 by benzyl isothiocyanate. Chem. Res. Toxicol. 12, 582–587.
Kent, U.M., E.S. Roberts, J. Chun, K. Hodge, J. Juncaj, and P.F. Hollenberg (1998). Inactivation of cytochrome P450 2E1 by tert-butylisothiocyanate. Chem. Res. Toxicol. 11, 1154–1161.
Chen, L., M. Lee, J.Y. Hong, W. Huang, E. Wang, and C.S. Yang (1994). Relationship between cytochrome P450 2E1 and acetone catabolism in rats as studied with diallyl sulfide as an inhibitor. Biochem. Pharmacol. 48, 2199–2205.
Lin, M.C., E.J. Wang, C. Patten, M.J. Lee, F. Xiao, K.R. Reuhl et al. (1996). Protective effect of diallyl sulfone against acetaminophen-induced hepatotoxicity in mice. J. Biochem. Toxicol. 11, 11–20.
Premdas, P.D., R.J. Bowers, and P.G. Forkert (2000). Inactivation of hepatic CYP2E1 by an epoxide of diallyl sulfone. J. Pharmacol. Exp. Ther. 293, 1112–1120.
Langouet, S., L.L. Furge, N. Kerriguy, K. Nakamura, A. Guillouzo, and F.P. Guengerich (2000). Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, oltipraz and its derivatives, and sulforaphane. Chem. Res. Toxicol. 13, 245–252.
Underwood, M.C., J.R. Cashman, and M.A. Correia (1992). Specifically designed thiosteroids as active site-directed probes for functional dissection of cytochrome P-450 3A isozymes. Chem. Res. Tox. 5, 42–53.
Stevens, J.C. and J. Halpert (1988). Selective inactivation of four rat liver microsomal androstenedione hydroxylases by chloramphenicol analogs. Mol. Pharmacol. 33, 103–110.
Halpert, J., J.Y. Jaw, L. Cornfield, C. Balfour, and E.A. Mash (1989). Selective inactivation of rat liver cytochromes P-450 by 21-chlorinated steroids. Drug Metab. Dispos. 17, 26–31.
Halpert, J., J.Y. Jaw, C. Balfour, E.A. Mash, and E.F. Johnson (1988). Selective inactivation by 21-chlorinated steroids of rabbit liver and adrenal microsomal cytochromes P-450 involved in progesterone hydroxylation. Arch. Biochem. Biophys. 264, 462–471.
Ortiz de Montellano, P.R. (1985). Alkenes and alkynes. In M. Anders (ed.), Bioactivation of Foreign Compounds. Academic Press, New York, pp. 121–155.
De Matteis, F. (1978). Loss of liver cytochrome P-450 caused by chemicals. In F. De Matteis and W.N. Aldridge (eds.), Heme and Hemoproteins, Handbook of Experimental Pharmacology, Vol. 44. Springer-Verlag, Berlin, pp. 95–127.
Ortiz de Montellano, P.R. and M.A. Correia (1983). Suicidal destruction of cytochrome P-450 during oxidative drug metabolism. Ann. Rev. Pharmacol. Toxicol. 23, 481–503.
Ortiz de Montellano, P.R. and B.A. Mico (1980). Destruction of cytochrome P-450 by ethylene and other olefins. Mol. Pharmacol. 18, 128–135.
He, K., A.M. Falick, B. Chen, F. Nilsson, and M.A. Correia (1996). Identification of the heme adduct and an active site peptide modified during mechanism-based inactivation of rat liver cytochrome P450 2B1 by secobarbital. Chem. Res. Toxicol. 9, 614–622.
He, K., Y.A. He, G. Szklarz, J.R. Halpert, and M.A. Correia (1996). Secobarbital-mediated inactivation of cytochrome P450 2B1 and its active site mutants: Partitioning between heme and protein alkylation and epoxidation. J. Biol. Chem. 271, 25864–25872.
Lukton, D., J.E. Mackie, J.S. Lee, G.S. Marks, and P.R. Ortiz de Montellano (1988). 2,2-Dialkyl-1,2-dihydroquinolines: Cytochrome P-450 catalyzed N-alkylporphyrin formation, ferrochelatase inhibition, and induction of 5-aminolevulinic acid synthase activity. Chem. Res. Toxicol. 1, 208–215.
Poulos, T.L., J.R. Cupp-Vickery, and H. Li (1995). In P.R. Ortiz de Montellano (ed.), Cytochrome P450: Structure, Mechanism and Biochemistry. Plenum Press, New York, pp. 125–150.
Gotoh, O. (1992). Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267, 83–90.
Nelson, D.R. and H.W. Strobel (1988). On the membrane topology of vertebrate cytochrome P-450 proteins. J. Biol. Chem. 263, 6038–6050.
von Wachenfeldt, C. and E.F. Johnson (1995). Structures of eukaryotic cytochrome P450 enzymes, In P.R. Ortiz de Montellano (ed.), Cytochrome P450: Structure, Mechanism and Biochemistry. Plenum Press, New York, pp. 183–223.
Ortiz de Montellano, P.R. and E.A. Komives (1985). Branchpoint for heme alkylation and metabolite formation in the oxidation of aryl acetylenes. J. Biol. Chem. 260, 3330–3336.
Roberts, E.S., S.J. Pernecky, W.L. Alworth, and P.F. Hollenberg (1996). A role for threonine 302 in the mechanism-based inactivation of P450 2B4 by 2-ethynylnaphthalene. Arch. Biochem. Biophys. 331, 170–176.
Ullrich, V. and P. Weber (1972). The O-dealkylation of 7-ethoxycoumarin by liver microsomes. A direct fluorometric test. Hoppe-Seyler’s Z. Physiol. Chem. 353, 1171–1177.
Buters, J.T., C.D. Schiller, and R.C. Chou (1993). A highly sensitive tool for the assay of cytochrome P450 enzyme activity in rat, dog and man. Direct fluorescence monitoring of the deethylation of 7-ethoxy-4-trifluoromethylcoumarin. Biochem. Pharmacol. 46, 1577–1584.
Yu, P.H., B.A. Davis, and A.A. Boulton (1993). Effect of structural modification of alkyl N-propargylamines on the selective inhibition of monoamine oxidase B activity. Biochem. Pharmacol. 46, 753–757.
Sharma, U., E.S. Roberts, and P.F. Hollenberg (1996). Inactivation of cytochrome P4502B1 by the monoamine oxidase inhibitors R-(−)-deprenyl and clorgyline. Drug Metab. Dispos. 24, 669–675.
Dyck, L.E. and B.A. Davis (2001). Inhibition of rat liver microsomal CYP1A2 and CYP2B1 activity by N-(2-heptyl)-N-methyl-propargylamine and by N-(2-heptyl)-propargylamine. Drug Metab. Dispos. 29, 1156–1161.
Cutler, A.J., P.A. Rose, T.M. Squires, M.K. Loewen, A.C. Shaw, J.W. Quail et al. (2000). Inhibitors of abscisic acid 8′-hydroxylase. Biochemistry 39, 13614–13624.
Crowley, J.R. and P.F. Hollenberg (1995). Mechanism-based inactivation of rat liver cytochrome P4502B1 by phencyclidine and its oxidative product, the iminium ion. Drug Metab. Dispos. 23, 786–793.
Jushchyshyn, M.I., U.M. Kent, and P.F. Hollenberg (2003). The mechanism-based inactivation of human cytochrome P450 2B6 by phencyclidine. Drug Metab. Dispos. 31, 46–52.
Ward, D.P., A.J. Trevor, A. Kalir, J.D. Adams, T.A. Baillie, and N. Castagnoli (1982). Metabolism of phencyclidine. The role of iminium ion formation in covalent binding to rabbit microsomal protein. Drug Metab. Dispos. 10, 690–695.
Hoag, M.K., A.J. Trevor, Y. Asscher, J. Weissman, and N. Castagnoli (1984). Metabolism-dependent inactivation of liver microsomal enzymes by phencyclidine. Drug Metab. Dispos. 12, 371–375.
Hoag, M.K.P., A.J. Trevor, A. Kalir, and N. Castagnoli (1987). NADPH-dependent metabolism, covalent binding to macromolecules, and inactivation of cytochrome(s) P450. Drug Metab. Dispos. 15, 485–490.
Owens, S.M., M. Gunnell, E.M. Laurenzana, and J.L. Valentine (1993). Dose-and time-dependent changes in phencyclidine metabolite covalent binding in rats and the possible role of CYP2D1. J. Pharmacol. Exp. Ther. 265, 1261–1266.
Hoag, M.K., M. Schmidt-Peetz, P. Lampen, A. Trevor, and N. Castagnoli (1988). Metabolic studies on phencyclidine: Characterization of a phencyclidine iminium ion metabolite. Chem. Res. Toxicol. 1, 128–131.
Osawa, Y. and M.J. Coon (1989). Selective mechanism-based inactivation of the major phenobarbital-inducible P-450 cytochrome from rabbit liver by phencyclidine and its oxidation product, the iminium compound. Drug Metab. Dispos. 17, 7–13.
Hiratsuka, A., T.Y. Chu, E.W. Distefano, L.Y. Lin, D.A. Schmitz, and A.K. Cho (1995). Inactivation of constitutive hepatic cytochromes P450 by phencyclidine in the rat. Drug Metab. Dispos. 23, 201–206.
Brady, J.F., J. Dokko, E.W. Di Stefano, and A.K. Cho (1987). Mechanism-based inhibition of cytochrome P-450 by heterocyclic analogues of phencyclidine. Drug Metab. Dispos. 15, 648–652.
Sharma, U., E.S. Roberts, U.M. Kent, S.M. Owens, and P.F. Hollenberg (1997). Metabolic inactivation of cytochrome P4502B1 by phencyclidine: Immunochemical and radiochemical analyses of the protective effects of glutathione. Drug Metab. Dispos. 25, 243–250.
Bornheim, L.M., E.T. Everhart, J. Li, and M.A. Correia (1993). Characterization of cannabidiol-mediated cytochrome P450 inactivation. Biochem. Pharmacol. 45, 1323–1331.
Bornheim, L.M. and M.P. Grillo (1998). Characterization of cytochrome P450 3A inactivation by cannabidiol: Possible involvement of cannabidiol-hydroxyquinone as a P450 inactivator. Chem. Res. Toxicol. 11, 1209–1216.
Watanabe, K., N. Usami, I. Yamamoto, and H. Yoshimura (1991). Inhibitory effect of cannabidiol hydroxy-quinone, an oxidative product of cannabidiol, on the hepatic microsomal drugmetabolizing enzymes of mice. J. Pharmacobiodyn. 14, 421–427.
Bornheim, L.M. (2000). Effects of unsaturated sidechain analogs of tetrahydrocannabinol on cytochromes P450. Biochem. Pharmacol. 60, 955–961.
Pathak, M.A., F. Daniels, and T.B. Fitzpatrick (1962). The presently known distribution of furocoumarins (psoralens) in plants. J. Invest. Dermatol. 38, 225–239.
Koenigs, L.L., R.M. Peter, S.J. Thompson, A.E. Rettie, and W.F. Trager (1997). Mechanism-based inactivation of human liver cytochrome P450 2A6 by 8-methoxypsoralen. Drug Metab. Dispos. 25, 1407–1415.
Fuhr, U. (1998). Drug interactions with grapefruit juice. Extent, probable mechanism and clinical relevance. Drug Saf. 18, 251–272.
Lin, J.H., M. Chiba, I.W. Chen, K.J. Vastag, J.A. Nishime, B.D. Dorsey et al. (1995). Time-and dose-dependent pharmacokinetics of L-754,394, an HIV protease inhibitor, in rats, dogs and monkeys. J. Pharmacol. Exp. Ther. 274, 264–269.
Zhang, F., P.W. Fan, X. Liu, L. Shen, R.B. van Breeman, and J.L. Bolton (2000). Synthesis and reactivity of a potential carcinogenic metabolite of tamoxifen: 3,4-dihydroxytamoxifen-o-quinone. Chem. Res. Toxicol. 13, 53–62.
Pirmohamed, M., N.R. Kitteringham, T.M. Guenthner, A.M. Breckenridge, and B.K. Park (1992). An investigation of the formation of cytotoxic, protein-reactive and stable metabolites from carbamazepine in vitro. Biochem. Pharmacol. 43, 1675–1682.
Madden, S., J.L. Maggs, and B.K. Park (1996). Bioactivation of carbamazepine in the rat in vivo. Evidence for the formation of reactive arene oxide(s). Drug Metab. Dispos. 24, 469–479.
Furst, S.M., P. Sukhai, R.A. McClelland, and J.P. Uetrecht (1995). Covalent binding of carbamazepine oxidative metabolites to neutrophils. Drug Metab. Dispos. 23, 590–594.
Ju, C. and J.P. Uetrecht (1999). Detection of 2-hydroxyiminostilbene in the urine of patients taking carbamazepine and its oxidation to a reactive iminoquinone intermediate. J. Pharmacol. Exp. Ther. 288, 51–56.
Wolkenstein, P., C. Tan, S. Lecoeur, J. Wechsler, N. Garcia-Martin, D. Charue et al. (1998). Covalent binding of carbamazepine reactive metabolites to P450 isoforms present in the skin. Chem. Biol. Interact. 113, 39–50.
Pirmohamed, M., A. Graham, P. Roberts, D. Smith, D. Chadwick, A.M. Breckenridge et al. (1991). Carbamazepine-hypersensitivity: Assessment of clinical and in vitro chemical cross-reactivity with phenytoin and oxcarbazepine. Br. J. Clin. Pharmacol. 32, 741–749.
Riley, R.J., G. Smith, C.R. Wolf, V.A. Cook, and J.S. Leeder (1993). Human anti-endoplasmic reticulum autoantibodies produced in aromatic anticonvulsant hypersensitivity reactions recognise rodent CYP3A proteins and a similarly regulated human P450 enzyme(s). Biochem. Biophys. Res. Commun. 191, 32–40.
Leeder, J.S., A. Gaedigk, X. Lu, and V.A. Cook (1996). Epitope mapping studies with human anticytochrome P450 3A antibodies. Mol. Pharmacol. 49, 234–243.
Ueng, Y.F., T. Kuwabara, Y.J. Chun, and F.P. Guengerich (1997). Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36, 370–381.
Kang, P., S.L. Leeder, and M.A. Correia (2003). CYP3A4-mediated bioactivation of carbamazepine. In Proceedings, 12th North American ISSX Meeting. Providence, Rhode Island. p. 107.
Casida, J.E. (1970). Mixed-function oxidase involvement in the biochemistry of insecticide synergists. J. Agric. Food Chem. 18, 753–772.
Hodgson, E. and R.M. Philpot (1974). Interaction of methylenedioxyphenyl (1,3-benzodioxole) compounds with enzymes and their effects on mammals. Drug Metab. Rev. 3, 231–301.
Wilkinson, C.F., M. Murray, and C.B. Marcus (1984). Interactions of methylenedioxyphenyl compounds with cytochrome P-450 and effects on microsomal oxidation. In E. Hodgson, J.R. Bend, and R.M. Philpot (eds.), Reviews in Biochemical Toxicology, Vol. 6. Elsevier, Amsterdam, pp. 27–63.
Kulkarni, A.P., and E. Hodgson (1978). Cumene hydroperoxide-generated spectral interactions of piperonyl butoxide and other synergists with microsomes from mammals and insects. Pest. Biochem. Physiol. 9, 75–83.
Elcombe, C.R., J.W. Bridges, R.H. Nimmo-Smith, and J. Werringloer (1975). Cumene hydroperoxide-mediated formation of inhibited complexes of methylenedioxyphenyl compounds with cytochrome P-450. Biochem. Soc. Trans. 3, 967–970.
Franklin, M.R. (1971). The enzymic formation of a methylene dioxyphenyl derivative exhibiting an isocyanide-like spectrum with reduced cytochrome P-450 in hepatic microsomes. Xenobiotica 1, 581–591.
Elcombe, C.R., J.W. Bridges, T.J.B. Gray, R.H. Nimmo-Smith, and K.J. Netter (1975). Studies on the interaction of safrole with rat hepatic microsomes. Biochem. Pharmacol. 24, 1427–1433.
Dickins, M., C.R. Elcombe, S.J. Moloney, K.J. Netter, and J.W. Bridges (1979). Further studies on the dissociation of the isosafrole metabolite-cytochrome P-450 complex. Biochem. Pharmacol. 28, 231–238.
Ullrich, V. and K.H. Schnabel (1973). Formation and binding of carbanions by cytochrome P-450 of liver microsomes. Drug Metab. Dispos. 1, 176–183.
Ullrich, V. (1977). Mechanism of microsomal monooxygenases and drug toxicity. In D.J. Jollow, J. Kocsis, R. Snyder, and H. Vaino (eds.), Biological Reactive Intermediates, Plenum Press, New York, pp. 65–82.
Murray, M., K. Hetnarski, and C.F. Wilkinson (1985). Selective inhibitory interactions of alkoxymethylenedioxybenzenes towards monooxygenase activity in rat-hepatic microsomes. Xenobiotica 15, 369–379.
Murray, M., C.F. Wilkinson, C. Marcus, and C.E. Dube (1983). Structure-activity relationships in the interactions of alkoxymethylenedioxybenzene derivatives with rat hepatic microsomal mixed-function oxidases in vivo. Mol. Pharmacol. 24, 129–136.
Mansuy, D. (1981). Use of model systems in biochemical toxicology: Heme models. In E. Hodgson, J.R. Bend, and R.M. Philpot (eds.), Reviews in Biochemical Toxicology, Vol. 3. Elsevier, Amsterdam, pp. 283–320.
Mansuy, D., J.P. Battioni, J.C. Chottard, and V. Ullrich (1979). Preparation of a porphyrin-ironcarbene model for the cytochrome P-450 complexes obtained upon metabolic oxidation of the insecticide synergists of the 1,3-benzodioxole series. J. Am. Chem. Soc. 101, 3971–3973.
Dahl, A.R. and E. Hodgson (1979). The interaction of aliphatic analogs of methylenedioxyphenyl compounds with cytochromes P-450 and P-420. Chem. Biol. Interact. 27, 163–175.
Anders, M.W., J.M. Sunram, and C.F. Wilkinson (1984). Mechanism of the metabolism of 1,3-benzodioxoles to carbon monoxide. Biochem. Pharmacol. 33, 577–580.
Hansch, C. (1968). The use of homolytic, steric, and hydrophobic constants in a structure-activity study of 1,3-benzodioxole synergists. J. Med. Chem. 11, 920–924.
Hennessy, D.J. (1965). Hydride-transferring ability of methylene dioxybenzenes as a basis of synergistic activity. J. Agric Food Chem. 13, 218–231.
Cook, J.C. and E. Hodgson (1983). Induction of cytochrome P-450 by methylenedioxyphenyl compounds: Importance of the methylene carbon. Toxicol. Appl. Pharmacol. 68, 131–139.
Casida, J.E., J.L Engel, E.G. Essac, F.X. Kamienski, and S. Kuwatsuka (1966). Methylene 14C-dioxyphenyl compounds: Metabolism in relation to their synergistic action. Science 153, 1130–1133.
Kamienski, F.X. and J.E. Casida (1970). Importance of methylenation in the metabolism in vivo and in vitro of methylenedioxyphenyl synergists and related compounds in mammals. Biochem. Pharmacol. 19, 91–112.
Yu, L.-S., C.F. Wilkinson, and M.W. Anders (1980). Generation of carbon monoxide during the microsomal metabolism of methylenedioxyphenyl compounds. Biochem. Pharmacol. 29, 1113–1122.
Metcalf, R.L., C.W. Fukuto, S. Fahmy, S. El-Azis, and E.R. Metcalf (1966). Mode of action of carbamate synergists. J. Agric Food. Chem. 14, 555–562.
Greenblatt, D.J., L.L. von Moltke, J.S. Harmatz, and R.I. Shader (1999). Human cytochromes and some newer antidepressants: Kinetics, metabolism, and drug interactions. J. Clin. Psychopharmacol. 19(Suppl 1), 23S–35S.
Belpaire, F.M., P. Wijnant, A. Temmerman, B.B. Rasmussen, and K. Brosen (1998). The oxidative metabolism of metoprolol in human liver microsomes: Inhibition by the selective serotonin reuptake inhibitors. Eur. J. Clin. Pharmacol. 54, 261–264.
Otton, S.V., S.E. Ball, S.W. Cheung, T. Inaba, R.L. Rudolph, and E.M. Sellers (1996). Venlafaxine oxidation in vitro is catalysed by CYP2D6. Br. J. Clin. Pharmacol. 41, 149–156.
Bloomer, J.C., F.R. Woods, R.E. Haddock, M.S. Lennard, and G.T. Tucker (1992). The role of cytochrome P4502D6 in the metabolism of paroxetine by human liver microsomes. Br. J. Clin. Pharmacol. 33, 521–523.
Sindrup, S.H., K. Brosen, and L.F. Gram (1992). Pharmacokinetics of the selective serotonin reuptake inhibitor paroxetine: Nonlinearity and relation to the sparteine oxidation polymorphism. Clin. Pharmacol. Ther. 51, 288–295.
Sindrup, S.H., K. Brosen, L.F. Gram, J. Hallas, E. Skjelbo, A. Allen et al. (1992). The relationship between paroxetine and the sparteine oxidation polymorphism. Clin. Pharmacol. Ther. 51, 278–287.
Bertelsen, K.M., K. Venkatakrishnan, L.L. Von Moltke, R.S. Obach, and D.J. Greenblatt (2003). Apparent mechanism-based inhibition of human CYP2D6 in vitro by paroxetine: Comparison with fluoxetine and quinidine. Drug Metab. Dispos. 31, 289–293.
Haddock, R.E., A.M. Johnson, P.F. Langley, D.R. Nelson, J.A. Pope, D.R. Thomas et al. (1989). Metabolic pathway of paroxetine in animals and man and the comparative pharmacological properties of its metabolites. Acta. Psychiatr. Scand. 80, 24–26.
Nakajima, M., M. Suzuki, R. Yamaji, H. Takashina, N. Shimada, H. Yamazaki et al. (1999). Isoform selective inhibition and inactivation of human cytochrome P450s by methylenedioxyphenyl compounds. Xenobiotica 29, 1191–1202.
Sharma, U., E.S. Roberts, and P.F. Hollenberg (1996). Formation of a metabolic intermediate complex of cytochrome P4502B1 by clorgyline. Drug Metab. Dispos. 24, 1247–1253.
Franklin, M.R. (1977). Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P-450 metabolic-intermediate complexes. Pharmacol. Ther. A. 2, 227–245.
Larrey, D., M. Tinel, and D. Pessayre (1983). Formation of inactive cytochrome P450 Fe(II)-metabolite complexes with several erythromycin derivatives but not with josamycin and midecamycin in rats. Biochem. Pharmacol. 32, 1487–1493.
Delaforge, M., M. Jaquen, and D. Mansuy (1983). Dual effects of macrolide antibiotics on rat liver cytochrome P-450. Induction and formation of metabolite-complexes: A structure-activity relationship. Biochem. Pharmacol. 32, 2309–2318.
Mansuy, D., P. Beaune, T. Cresteil, C. Bacot, J.C. Chottard, and P. Gans (1978). Formation of complexes between microsomal cytochrome P-450-Fe(II) and nitrosoarenes obtained by oxidation of arylhydroxylamines or reduction of nitroarenes in situ. Eur. J. Biochem. 86, 573–579.
Jonsson, J. and B. Lindeke (1976). On the formation of cytochrome P-450 product complexes during the metabolism of phenylalkylamines. Acta. Pharm. Suec. 13, 313–320.
Franklin, M.R. (1974). The formation of a 455 nm complex during cytochrome P-450-dependent N-hydroxylamphetamine metabolism. Mol. Pharmacol. 10, 975–985.
Mansuy, D. (1978). Coordination chemistry of cytochromes P-450 and iron-porphyrins: Relevance to pharmacology and toxicology. Biochimie. 60, 969–977.
Lindeke, B., E. Anderson, G. Lundkvist, H. Jonsson, and S.O. Eriksson (1975). Autoxidation of N-hydroxyamphetamine and N-hydroxyphentermine: The formation of 2-nitroso-1-phenylpropanes and 1-phenyl-2-propanone oxime. Acta Pharm. Suec. 12, 183–198.
Mansuy, D., P. Gans, J.C. Chottard. and J.F. Bartoli (1977). Nitrosoalkanes as Fe(II) ligands in the 455-nm-absorbing cytochrome P-450 complexes formed from nitroalkanes in reducing conditions. Eur. J. Biochem. 76, 607–615.
Pessayre, D., M. Konstantinova-Mitcheva, V. Descatoire, B. Cobert, J.C. Wandscheer, R. Level et al. (1981). Hypoactivity of cytochrome P-450 after triacetyloleandomycin administration. Biochem. Pharmacol. 30, 559–564.
Wrighton, S.A., P. Maurel, E.G. Schuetz, P.B. Watkins, B. Young, and P.S. Guzelian (1985). Identification of the cytochrome P-450 induced by macrolide antibiotics in rat liver as the glucocorticoid responsive cytochrome P-450p. Biochemistry 24, 2171–2178.
Watkins, P.B., S.A. Wrighton, E.G. Schuetz, P. Maurel, and P.S. Guzelian (1986). Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P-450p in rat hepatocytes in vivo and in primary monolayer culture. J. Biol. Chem. 261, 6264–6271.
Zhukov, A. and M. Ingelman-Sundberg (1999). Relationship between cytochrome P450 catalytic cycling and stability: Fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH-cytochrome P450 reductase. Biochem. J. 34, 453–458.
Goasduff, T. and A.I. Cederbaum (1999). NADPH-dependent microsomal electron transfer increases degradation of CYP2E1 by the proteasome complex: Role of reactive oxygen species. Arch. Biochem. Biophys. 370, 258–270.
Henderson, C.J., D.M. Otto, D. Carrie, M.A. Magnuson, A.W. McLaren, I. Rosewell et al. (2003). Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J. Biol. Chem. 278, 13480–13486.
Hines, R.N. and R.A. Prough (1980). The characterization of an inhibitory complex formed with cytochrome P-450 and a metabolite of 1,1-disubstituted hydrazines. J. Pharmacol. Ther. 214, 80–86.
Muakkasah, S.F., W.R. Bidlack, and W.C.T. Yang (1981). Mechanism of the inhibitory action of isoniazid on microsomal drug metabolism. Biochem. Pharmacol. 30, 1651–1658.
Moloney, S.J., B.J. Snider, and R.A. Prough (1984). The interactions of hydrazine derivatives with rat-hepatic cytochrome P-450. Xenobiotica 14, 803–814.
Muakkassah, S.F., W.R. Bidlack, and W.C.T. Yang (1982). Reversal of the effects of isoniazid on hepatic cytochrome P-450 by potassium ferricyanide. Biochem. Pharmacol. 31, 249–251.
Mahy, J.P., P. Battioni, D. Mansuy, J. Fisher, R. Weiss, J. Mispelter et al. (1984). Iron porphyrin-nitrene complexes: Preparation from 1,1-dialkylhydrzines: Electronic structure from NMR, Mössbauer, and magnetic susceptibility studies and crystal structure of the [tetrakis p-chlorophenyl) porphyrinato-(2,2,6,6-tetramethyl-1-piperidyl) nitrene]iron complex. J. Am. Chem. Soc. 106, 1699–1706.
Mansuy, D., P. Battioni, and J.P. Mahy (1982). Isolation of an iron-nitrene complex from the dioxygen and iron porphyrin dependent oxidation of a hydrazine. J. Am. Chem. Soc. 104, 4487–4489.
Collman, J.P., P.D. Hampton, and J.I. Brauman (1986). Stereochemical and mechanistic studies of the “suicide” event in biomimetic P-450 olefin epoxidation. J. Am. Chem. Soc. 108, 7861–7862.
Ortiz de Montellano, P.R., R.A. Stearns, and K.C. Langry (1984). The allylisopropylacetamide and novonal prosthetic heme adducts. Mol. Pharmacol. 25, 310–317.
Ortiz de Montellano, P.R., B.L.K. Mangold, C. Wheeler, K.L. Kunze, and N.O. Reich (1983). Stereochemistry of cytochrome P-450-catalyzed epoxidation and prosthetic heme alkylation. J. Biol. Chem. 258, 4208–4213.
Ortiz de Montellano, P.R., K.L. Kunze, H.S. Beilan, and C. Wheeler (1982). Destruction of cytochrome P-450 by vinyl fluoride, fluroxene, and acetylene: Evidence for a radical cation intermediate in olefin oxidation. Biochemistry 21, 1331–1339.
Kunze, K.L., B.L.K. Mangold, C. Wheeler, H.S. Beilan, and P.R. Ortiz de Montellano (1983). The cytochrome P-450 active site. J. Biol. Chem. 258, 4202–4207.
Brady, J.F., H. Ishizaki, J.M. Fukuto, M.C. Lin, A. Fadel, J.M. Gapac et al. (1991). Inhibition of cytochrome P-450 2E1 by diallyl sulfide and its metabolites. Chem. Res. Toxicol. 4, 642–647.
Collman, J.P., P.D. Hampton, and J.I. Brauman (1986). Stereochemical and mechanistic studies of the “suicide” event in biomimetic P-450 olefin epoxidation. J. Amer. Chem. Soc. 108, 7861–7862.
Collman, J.P., P.D. Hampton, and J.I. Brauman (1990). Suicide inactivation of cytochrome P-450 model compounds by terminal olefins. Part I: A mechanistic study of heme N-alkylation and epoxidation. J. Am. Chem. Soc. 112, 2977–2986.
Collman, J.P., P.D. Hampton, and J.I. Brauman (1990). Suicide inactivation of cytochrome P-450 compounds by terminal olefins. Part II: Steric and electronic effects in heme N-alkylation and epoxidation. J. Am. Chem. Soc. 112, 2986–2998.
Mansuy, D., L. Devocelle, I. Artaud, and J.P. Battioni (1985). Alkene oxidations by iodosylbenzene catalyzed by iron-porphyrins: Fate of the catalyst and formation of N-alkyl-porphyrin green pigments from monosubstituted alkenes as in cytochrome P-450. Nouv. J. Chim. 9, 711–716.
Artaud, I., L. Devocelle, J.-P. Battioni, J.-P. Girault, and D. Mansuy (1987). Suicidal inactivation of iron porphyrin catalysts during alk-1-ene oxidation: Isolation of a new type of N-alkylporphyrin. J. Am. Chem. Soc. 109, 3782–3783.
Traylor, T.G., T. Nakano, A.R. Mikztal, and B.E. Dunlap (1987). Transient formation of N-alkyl-hemins during hemin-catalyzed epoxidation of norbornene. Evidence concerning the mechanisms of epoxidation. J. Am. Chem. Soc. 109, 3625–3632.
Traylor, T.G., and A.R. Mikztal (1989). Alkene epoxidations catalyzed by iron(III), manganese(III), and chromium(III) porphyrins. Effects of metal and porphyrin substituents on selectivity and regiochemistry of epoxidation. J. Am. Chem. Soc. 111, 7443–7448.
Nakano, T., T.G. Traylor, and D. Dolphin (1990). The formation of N-alkylporphyrins during epoxidation of ethylene catalyzed by iron(III) mesotetrakis(2,6-dichlorophenyl)porphyrin. Can J Chem. 10, 1859–1866.
Tian, Z.Q., J.L. Richards, and T.G. Traylor (1995). Formation of both primary and secondary N-alkylhemins during hemin-catalyzed epoxidation of terminal alkenes. J. Am. Chem. Soc. 117, 21–29.
Blobaum, A.L., U.M. Kent, and P.F. Hollenberg (2003). Novel reversible adduction of the P450 heme: Inactivation of cytochrome P450 2E1 T303A by tert-butyl acetylene. In Proceedings of the 13th International Conference on Cytochromes P450. Prague, Czech Republic, p. S173.
Dexter, A.F. and L.P. Hager (1995). Transient heme N-alkylation of chloroperoxidase by terminal alkenes and alkynes. J. Am. Chem. Soc. 117, 817–818.
Shaik, S., S.P. de Visser, F. Ogliaro, H. Schwarz, and D. Schröder (2002). Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P450 revealed by theory. Curr. Opin. Chem. Biol. 6, 556–567.
Ortiz de Montellano, P.R., and K.L. Kunze (1980). Self-catalyzed inactivation of hepatic cytochrome P-450 by ethynyl substrates. J. Biol. Chem. 255, 5578–5585.
Foroozesh, M., G. Primrose, Z. Guo, L.C. Bell, W.L. Alworth, and F.P. Guengerich (1997). Aryl acetylenes as mechanism-based inhibitors of cytochrome P450-dependent monooxygenase enzymes. Chem. Res. Toxicol. 10, 91–102.
Reilly, P.E., R.J. Gomi, and S.R. Mason (1999). Mechanism-based inhibition of rat liver microsomal diazepam C3-hydroxylase by mifepristone associated with loss of spectrally detectable cytochrome P450. Chem. Biol. Interact. 118, 39–49.
Spitz, I.M. and C.W. Bardin (1993). Mifepristone (RU 486)—a modulator of progestin and glucocorticoid action. N. Engl. J. Med. 329, 404–412.
Burger, A., J.E. Clark, M. Nishimoto, A.S. Muerhoff, B.S. Masters, and P.R. Ortiz de Montellano (1993). Mechanism-based inhibitors of prostaglandin omega-hydroxylase: (R)-and (S)-12-hydroxy-16-heptadecynoic acid and 2,2-dimethyl-12-hydroxy-16-heptadecynoic acid. J. Med. Chem. 36, 1418–1424.
Fan, P.W., C. Gu, S.A. Marsh, and J.C. Stevens (2003). Mechanism-based inactivation of cytochrome P450 2B6 by a novel terminal acetylene inhibitor. Drug Metab. Dispos. 31, 28–36.
De Matteis, F., G. Abbritti, and A.H. Gibbs (1973). Decreased liver activity of porphyrin-metal chelatase in hepatic porphyria caused by 3,5-diethoxycarbonyl-1,4-dihydrocollidine: Studies in rats and mice. Biochem. J. 134, 717–727.
De Matteis, F. and A. Gibbs (1972). Stimulation of liver 5-aminolaevulinate synthetase by drugs and its relevance to drug-induced accumulation of cytochrome P-450. Biochem. J. 126, 1149–1160.
Gayarthri, A.K. and G. Padmanaban (1974). Biochemical effects of 3,5-diethoxycarbonyl-1,4-dihydrocollidine in mouse liver. Biochem. Pharmacol. 23, 2713–2725.
Tephly, T.R., A.H. Gibbs, G. Ingall, and F. De Matteis (1980). Studies on the mechanism of experimental porphyria and ferrochelatase inhibition produced by 3,5-diethoxycarbonyl-1,4-dihydrocollidine. Int. J. Biochem. 12, 993–998.
Cole, S.P. and G.S. Marks (1984). Ferrochelatase and N-alkylated porphyrins. Mol. Cell Biochem. 64, 127–137.
Ortiz de Montellano, P.R., H.S. Beilan, and K.L. Kunze (1981). N-Alkylprotoporphyrin IX formation in 3,5-dicarbethoxy-1,4-dihydrocollidine-treated rats. Transfer of the alkyl group from the substrate to the porphyrin. J. Biol. Chem. 256, 6708–6713.
Augusto, O., H.S. Beilan, and P.R. Ortiz de Montellano (1982). The catalytic mechanism of cytochrome P-450: Spin-trapping evidence for one-electron substrate oxidation. J. Biol. Chem. 257, 11288–11295.
De Matteis, F., C. Hollands, A.H. Gibbs, N. de Sa, and M. Rizzardini (1982). Inactivation of cytochrome P-450 and production of N-alkylated porphyrins caused in isolated hepatocytes by substituted dihydropyridines: Structural requirements for loss of haem and alkylation of the pyrrole nitrogen atom. FEBS Lett. 145, 87–92.
Tephly, T.R., B.L. Coffman, G. Ingall, M.S. Abou Zeit-Har, H.M. Goff, H.D. Tabba et al. (1981). Identification of N-methylprotoporphyrin IX in livers of untreated mice and mice treated with 3,5-diethoxycarbonyl-1,4-dihydrocollidine: Source of the methyl group. Arch. Biochem. Biophys. 212, 120–126.
De Matteis, F., A.H. Gibbs, P.B. Farmer, and J.H. Lamb (1981). Liver production of N-alkylated porphyrins caused by treatment with substituted dihydropyridines. FEBS Lett. 129, 328–331.
De Matteis, F., A.H. Gibbs, and C. Hollands (1983). N-Alkylation of the haem moiety of cytochrome P-450 caused by substituted dihydropyridines. Preferential attack of different pyrrole nitrogen atoms after induction of various cytochrome P-450 isoenzymes. Biochem. J. 211, 455–461.
McCluskey, S.A., G.S. Marks, E.P. Sutherland, N. Jacobsen, and P.R. Ortiz de Montellano (1986). Ferrochelatase-inhibitory activity and N-alkylprotoporphyrin formation with analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine (DDC) containing extended 4-alkyl groups: Implications for the active site of ferrochelatase. Mol. Pharmacol. 30, 352–357.
McCluskey, S.A., D.S. Riddick, J.E. Mackie, R.A. Kimmett, R.A. Whitney, and G.S. Marks (1992). Inactivation of cytochrome P450 and inhibition of ferrochelatase by analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine with 4-nonyl and 4-dodecyl substituents. Can. J. Physiol. Pharmacol. 70, 1069–1074.
Lee, J.S., N.E. Jacobsen, and P.R. Ortiz de Montellano (1988). 4-Alkyl radical extrusion in the cytochrome P-450-catalyzed oxidation of 4-alkyl-1,4-dihydropyridines. Biochemistry 27, 7703–7710.
Böcker, R.H. and F.P. Guengerich (1986). Oxidation of 4-aryl-and 4-alkyl-substituted 2,6-dimethyl-3,5-bis(alkoxycarbonyl)-1,4-dihydropyridines by human liver microsomes and immunochemical evidence for the involvement of a form of cytochrome P-450. J. Med. Chem. 29, 1596–1603.
Tephly, T.R., K.A. Black, M.D. Green, B.L. Coffman, G.A. Dannan, and F.P. Guengerich (1986). Effect of the suicide substrate 3,5-diethoxycarbonyl-2,6-dimethyl-4-ethyl-1,4-dihydropyridine on the metabolism of xenobiotics and on cytochrome P-450 apoproteins. Mol. Pharmacol. 29, 81–87.
Riddick, D.S., S.S. Park, H.V. Gelboin, and G.S. Marks (1990). Effects of 4-alkyl analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine on hepatic cytochrome P-450 heme, apoproteins, and catalytic activities following in vivo administration to rats. Mol. Pharmacol. 37, 130–136.
McCluskey, S.A., R.A. Whitney, and G.S. Marks (1989). Evidence for the stereoselective inhibition of chick embryo hepatic ferrochelatase by N-alkylated porphyrins. Mol. Pharmacol. 36, 608–614.
Kennedy, C.H. and R.P. Mason (1990). A reexamination of the cytochrome P-450-catalyzed free radical production from dihydropyridine: Evidence of trace transition metal catalysis. J. Biol. Chem. 265, 11425–11428.
Ortiz de Montellano, P.R. and D.E. Kerr (1985). Inactivation of myoglobin by ortho-substituted aryl hydrazines: Formation of prosthetic heme aryl-iron but not N-aryl adducts. Biochemistry 24, 1147–1152.
Lukton, D., J.E. Mackie, J.S. Lee, G.S. Marks, and P.R. Ortiz de Montellano (1988). 2,2-Dialkyl-1,2-dihydroquinolines: Cytochrome P-450 catalyzed N-alkylporphyrin formation, ferrochelatase inhibition, and induction of 5-aminolevulinic acid synthase activity. Chem. Res. Toxicol. 1, 208–215.
Muakkassah, W.F., and W.C.T. Yang (1981). Mechanism of the inhibitory action of phenelzine on microsomal drug metabolism. J. Pharmacol. Exp. Ther. 219, 147–155.
Ortiz de Montellano, P.R. O. Augusto, F. Viola, and K.L. Kunze (1983). Carbon radicals in the metabolism of alkyl hydrazines. J. Biol. Chem. 258, 8623–8629.
Ortiz de Montellano, P.R. and M.D. Watanabe (1987). Free radical pathways in the in vitro hepatic metabolism of phenelzine. Mol. Pharmacol. 31, 213–219.
Rumyantseva, G.V., C.H. Kennedy, and R.P. Mason (1991). Trace transition metal-catalyzed reactions in the microsomal metabolism of alkyl hydrazines to carbon-centered free radicals. J. Biol. Chem. 266, 21422–21427.
Jonen, H.G., J. Werringloer, R.A. Prough, and R.W. Estabrook (1982). The reaction of phenylhydrazine with microsomal cytochrome P-450: Catalysis of heme modification. J. Biol. Chem. 257, 4404–4411.
Mansuy, D., P. Battioni, J.F. Bartoli, and J.P. Mahy (1985). Suicidal inactivation of microsomal cytochrome P-450 by hydrazones. Biochem. Pharmacol. 34, 431–432.
Delaforge, M., P. Battioni, J.P. Mahy, and D. Mansuy (1986). In vivo formation of σ-methyl and σ-phenyl-ferric complexes of hemoglobin and liver cytochrome P-450 upon treatment of rats with methyl and phenylhydrazine. Chem. Biol. Interact. 60, 101–114.
Raag, R., B.S. Swanson, T.L. Poulos, and P.R. Ortiz de Montellano (1990). Formation, crystal structure, and rearrangement of a cytochrome P450cam ironphenyl complex. Biochemistry, 29, 8119–8126.
Ortiz de Montellano, P.R. and K.L. Kunze (1981). Formation of N-phenylheme in the hemolytic reaction of phenylhydrazine with hemoglobin. J. Am. Chem. Soc. 103, 581–586.
Saito, S. and H.A. Itano (1981). Beta-mesophenylbiliverdin IX-alpha and N-phenylprotoporphyrin IX, products of the reaction of phenylhydrazine with oxyhemoproteins. Proc. Natl. Acad. Sci. USA 78, 5508–5512.
Augusto, O., K.L. Kunze, and P.R. Ortiz de Montellano (1982). N-Phenylprotoporphyrin IX formation in the hemoglobin-phenylhydrazine reaction: Evidence for a protein-stabilized iron-phenyl intermediate. J. Biol. Chem. 257, 6231–6241.
Kunze, K.L. and P.R. Ortiz de Montellano (1983). Formation of a sigma-bonded aryl-iron complex in the reaction of arylhydrazines with hemoglobin and myoglobin. J. Am. Chem. Soc. 105, 1380–1381.
Ortiz de Montellano, P.R. and D.E. Kerr (1983). Inactivation of catalase by phenylhydrazine: Formation of a stable aryl-iron heme complex. J. Biol. Chem. 258, 10558–10563.
Ringe, D., G.A. Petsko, D.E. Kerr, and P.R. Ortiz de Montellano (1984). Reaction of myoglobin with phenylhydrazine: A molecular doorstop. Biochemistry 23, 2–4.
Swanson, B.A. and P.R. Ortiz de Montellano (1991). Structure determination and absolute stereochemistry of the four N-phenylprotoporphyrin IX regioisomers. J. Am. Chem. Soc. 113, 8146–8153.
Tuck, S.F., S. Graham-Lorence, J.A. Peterson, and P.R. Ortiz de Montellano (1993). Active sites of the cytochrome P450cam (CYP101) F87W and F87A mutants. Evidence for significant structural reorganization without alteration of catalytic regio-specificity. J. Biol. Chem. 268, 269–275.
Swanson, B.A., D.R. Dutton, C.S. Yang, and P.R. Ortiz de Montellano (1991). The active sites of cytochromes P450 IA1, IIB1, IIB2, and IIE1. Topological analysis by in situ rearrangement of phenyl-iron complexes J. Biol. Chem. 266, 19258–19264.
Swanson, B.A., J.R. Halpert, L.M. Bornheim, and P.R. Ortiz de Montellano (1992). Topological analysis of the active sites of cytochromes P450IIB4 (rabbit), P450IIB10 (mouse) and P450IIB11 (dog) by in situ rearrangement of phenyl-iron complexes. Arch. Biochem. Biophys. 292, 42–46.
Tuck, S.F., J.A. Peterson, and P.R. Ortiz de Montellano (1992). Active site topologies of bacterial cytochromes P450 101 (P450cam), P450 108 (P450terp), and P450 102 (P450BM-3): In situ rearrangement of their phenyl-iron complexes. J. Biol. Chem. 267, 5614–5620.
Tuck, S.F., Y. Aoyama, Y. Yoshida, and P.R. Ortiz de Montellano (1992). Active site topology of Saccharomyces cerevisiae lanosterol 14α-demethylase (CYP51) and its A310D mutant (cytochrome P450SG1). J. Biol. Chem. 267, 13175–13179.
Tuck, S.F., and P.R. Ortiz de Montellano (1992). Topological mapping of the active sites of cytochromes P4502B1 and P4502B2 by in situ rearrangement of their aryl-iron complexes. Biochemistry 31, 6911–6916.
Tuck, S.F., K. Hiroya, T. Shimizu, M. Hatano, and P.R. Ortiz de Montellano (1993). The cytochrome P450 1A2 (CYP1A2) active site: Topology and perturbations caused by Glu-318 and Thr-319 mutations. Biochemistry 32, 2548–2553.
Battioni, P., J.P. Mahy, M. Delaforge, and D. Mansuy (1983). Reaction of monosubstituted hydrazines and diazenes with rat-liver cytochrome P-450: Formation of ferrous-diazene and ferric sigma-alkyl complexes. Eur. J. Biochem. 134, 241–248.
Battioni, P., J.-P. Mahy, G. Gillet, and D. Mansuy (1983). Iron porphyrin dependent oxidation of methyl-and phenylhydrazine: Isolation of iron(II)-diazene and sigma-alkyliron (III) (or aryliron(III)) complexes. Relevance to the reactions of hemoproteins with hydrazines. J. Am. Chem. Soc. 105, 1399–1401.
Masubuchi, Y. and T. Horie (1998). Dihydralazine-induced inactivation of cytochrome P450 enzymes in rat liver microsomes. Drug Metab. Dispos. 26, 338–342.
Masubuchi, Y. and T. Horie (1999). Mechanism-based inactivation of cytochrome P450s 1A2 and 3A4 by dihydralazine in human liver microsomes. Chem. Res. Toxicol. 12, 1028–1032.
Bourdi, M., J.C. Gautier, J. Mircheva, D. Larrey, A. Guillouzo, C. Andreet al. (1992). Anti-liver microsomes autoantibodies and dihydralazine-induced hepatitis: Specificity of autoantibodies and inductive capacity of the drug. Mol. Pharmacol. 42, 280–285.
Belloc, C., A. Gauffre, C. Andre, and P.H. Beaune (1997). Epitope mapping of human CYP1A2 in dihydralazine-induced autoimmune hepatitis. Pharmacogenetics 7, 181–186.
Campbell, C.D. and C.W. Rees (1969). Reactive intermediates. Part III. Oxidation of 1-aminobenzotriazole with oxidants other than lead tetra-acetate. J. Chem. Soc. Chem. Commun. 752–756.
Ortiz de Montellano, P.R. and J.M. Mathews (1981). Autocatalytic alkylation of the cytochrome P-450 prosthetic haem group by 1-aminobenzotriazole: Isolation of an N,N-bridged benzyne-protoporphyrin IX adduct. Biochem. J. 195, 761–764.
Ortiz de Montellano, P.R., J.M. Mathews, and K.C. Langry (1984). Autocatalytic inactivation of cytochrome P-450 and chloroperoxidase by 1-amino-benzotriazole and other aryne precursors. Tetrahedron 40, 511–519.
Mathews, J.M. and J.R. Bend (1986). N-Alkylaminobenzotriazoles as isozyme-selective suicide inhibitors of rabbit pulmonary microsomal cytochrome P-450. Mol. Pharmacol. 30, 25–32.
Mathews, J.M. and J.R. Bend (1993). N-Aralkyl derivatives of 1-aminobenzotriazole as potent isozyme-selective mechanism-based inhibitors of rabbit pulmonary cytochrome P450 in vivo. J. Pharmacol. Exp. Ther. 265, 281–285.
Ortiz de Montellano, P.R. and A.K. Costa (1985). Dissociation of cytochrome P450 inactivation and induction. Arch. Biochem. Biophys. 251, 514–524.
Mico, B.A., D.A. Federowicz, M.G. Ripple, and W. Kerns (1988). In vivo inhibition of oxidative drug metabolism by, and acute toxicity of, 1-aminobenzotriazole (ABT). Biochem. Pharmacol. 37, 2515–2519.
Mugford, C.A., M. Mortillo, B.A. Mico, and J.B. Tarloff (1992). 1-Aminobenzotriazole-induced destruction of hepatic and renal cytochromes P450 in male Sprague-Dawley rats. Fundam. Appl. Toxicol. 19, 43–49.
Xu, D., J.M. Voigt, B.A. Mico, S. Kominami, S. Takemori, and H.D. Colby (1994). Inhibition of adrenal cytochromes P450 by 1-aminobenzotriazole in vitro. Selectivity for xenobiotic metabolism. Biochem. Pharmacol. 48, 1421–1426.
Colby, H.D., B. Abbott, M. Cachovic, K.M. Debolt, and B.A. Mico (1995). Inactivation of adrenal cytochromes P450 by 1-aminobenzotriazole. Divergence of in vivo and in vitro actions. Biochem. Pharmacol. 49, 1057–1062.
Woodcroft, K.J., E.W. Szczepan, L.C. Knickle, and J.R. Bend (1990). Three N-aralkylated derivatives of 1-aminobenzotriazole as potent isozyme-selective mechanism-based inhibitors of guinea pig pulmonary cytochrome P450 in vitro. Drug Metab. Dispos. 18, 1031–1037.
Sinal, C.J. and J.R. Bend (1996). Kinetics and selectivity of mechanism-based inhibition of guinea pig hepatic and pulmonary cytochrome P450 by N-benzyl-1-aminobenzotriazole and N-alpha-methylbenzyl-1-aminobenzotriazole. Drug Metab. Dispos. 24, 996–1001.
Sinal, C.J., M. Hirst, C.D. Webb, and J.R. Bend (1998). Enantioselective, mechanism-based inactivation of guinea pig hepatic cytochrome P450 by N-(alpha-methylbenzyl)-1-aminobenzotriazole. Drug Metab. Dispos. 26, 681–688.
Sinal, C.J. and J.R. Bend (1995). Isozyme-selective metabolic intermediate complex formation of guinea pig hepatic cytochrome P450 by N-aralkylated derivatives of 1-aminobenzotriazole. Chem. Res. Toxicol. 8, 82–91.
Moreland, D.E., F.T. Corbin, and J.E. McFarland (1993). Effects of safeners on the oxidation of multiple substrates by grain sorghum microsomes. Pest. Biochem. Physiol. 45, 43–53.
Cabanne, F., D. Huby, P. Gaillardon, R. Scalla, and F. Durst (1987). Effect of the cytochrome P-450 inactivator 1-aminobenzotriazole on the metabolism of chlortoluron and isoproturon in wheat. Pest. Biochem. Biophys. 28, 371–380.
Feyereisen, R., K.C. Langry, and P.R. Ortiz de Montellano (1984). Self-catalyzed destruction of insect cytochrome P-450. Insect Biochem. 14, 19–26.
Capello, S., L. Henderson, F. DeGrazia, D. Liberato, W. Garland, and C. Town (1990). The effect of the cytochrome P-450 suicide inactivator, 1-aminobenzotriazole, on the in vivo metabolism and pharmacologic activity of flurazepam. Drug Metab. Dispos. 18, 190–196.
Kaikaus, R.M., W.K. Chan, N. Lysenko, R. Ray, P.R. Ortiz de Montellano, and N.M. Bass (1993). Induction of peroxisomal fatty acid β-oxidation and liver fatty acid-binding protein by peroxisome proliferators: Mediation via the cytochrome P450IVA1 ω-hydroxylase pathway. J. Biol. Chem. 268, 9593–9603.
Su, P., K.M. Kaushal, and D.L. Kroetz (1998). Inhibition of renal arachidonic acid omega-hydroxylase activity with ABT reduces blood pressure in the SHR. Am. J. Physiol. 275, R426–R438.
Whitman, D.W. and B.K. Carpenter (1980). Experimental evidence for nonsquare cyclobutadiene as a chemically significant intermediate in solution. J. Am. Chem. Soc. 102, 4272–4274.
Stearns, R.A. and P.R. Ortiz de Montellano (1985). Inactivation of cytochrome P450 by a catalytically generated cyclobutadiene species. J. Am. Chem. Soc. 107, 234–240.
Stejskal, R., M. Itabashi, J. Stanek, and Z. Hruban (1975). Experimental porphyria induced by 3-[2-(2,4,6-trimethylphenyl)-thioethyl]-4-methyl-sydnone. Virchows Arch. 18, 83–100.
Ortiz de Montellano, P.R. and L.A. Grab (1986). Inactivation of cytochrome P-450 during catalytic oxidation of a 3-[(arylthio)ethyl]sydnone: N-vinyl heme formation via insertion into the Fe-N bond. J. Am. Chem. Soc. 108, 5584–5589.
White, E.H. and N. Egger (1984). Reaction of sydnones with ozone as a method of deamination: On the mechanism of inhibition of monoamine oxidase by sydnones. J. Am. Chem. Soc. 106, 3701–3703.
Chevrier, B., R. Weiss, M.C. Lange, J.C. Chottard, and D. Mansuy (1981). An iron(III)-porphyrin complex with a vinylidene group inserted into an iron-nitrogen bond: Relevance of the structure of the active oxygen complex of catalase. J. Am. Chem. Soc. 103, 2899–2901.
Latos-Grazynski, L., R.J. Cheng, G.N. La Mar, and A.L. Balch (1981). Reversible migration of an axial carbene ligand into an iron-nitrogen bond of a porphyrin: Implications for high oxidation states of heme enzymes and heme catabolism. J. Am. Chem. Soc. 103, 4271–4273.
Grab, L.A., B.A. Swanson, and P.R. Ortiz de Montellano (1988). Cytochrome P-450 inactivation by 3-alkylsydnones: Mechanistic implications of N-alkyl and N-alkenyl heme adduct formation. Biochemistry 27, 4805–4814.
White, I.N.H., A.G. Smith, and P.B. Farmer (1983). Formation of N-alkylated protoporphyrin IX in the livers of mice after diethylnitrosamine treatment. Biochem. J. 212, 599–608.
Ding, X. and M.J. Coon (1988). Cytochrome P-450-dependent formation of ethylene from N-nitrosoethylamines. Drug Metab. Dispos. 16, 265–269.
Frater, Y., A. Brady, E.A. Lock, and F. De Matteis (1993). Formation of N-methyl protoporphyrin in chemically-induced protoporphyria. Studies with a novel porphyrogenic agent. Arch. Toxicol. 67, 179–185.
De Matteis, F. and A.H. Gibbs (1980). Drug-induced conversion of liver haem into modified porphyrins. Biochem. J. 187, 285–288.
Holley, A.E., Y. Frater, A.H. Gibbs, F. De Matteis, J.H. Lamb, P.B. Farmer et al. (1991). Isolation of two N-monosubstituted protoporphyrins, bearing either the whole drug or a methyl group on the pyrrole nitrogen atom, from liver of mice given griseofulvin. Biochem. J. 274, 843–848.
Gibbs, A.H., S. Naylor, J.H. Lamb, Y. Frater, F. De Matteis (1990). Copper-induced dealkylation studies of biologically N-alkylated porphyrins by fast atom bombardment mass spectrometry. Anal. Chim. Acta 241, 233–239.
De Matteis, F. and G.S. Marks (1996). Cytochrome P450 and its interactions with the heme biosynthetic pathway. Can. J. Physiol. Pharmacol. 74, 1–8.
Bellingham, R.M.A., A.H. Gibbs, F. De Matteis, L.-Y. Lian, and G.C.K. Roberts (1995). Determination of the structure of an N-substituted protoporphyrin isolated from the livers of griseofulvin-fed mice. Biochem. J. 307, 505–512.
Holley, A., L.J. King, A.H. Gibbs, and F. De Matteis (1990). Strain and sex differences in the response of mice to drugs that induce protoporphyria: Role of porphyrin biosynthesis and removal. J. Biochem. Toxicol. 5, 175–182.
De Matteis, F., A.H. Gibbs, S.R. Martin, and R.L.B. Milek (1991). Labeling in vivo and chirality of griseofulvin-derived N-alkylated protoporphyrins. Biochem. J. 280, 813–816.
Kobus, S.M., S.G. Wong, and G.S. Marks (2001). Isolation of regioisomers of N-alkylprotoporphyrin IX from chick embryo liver after treatment with porphyrinogenic xenobiotics. Can. J. Physiol. Pharmacol. 79, 814–821.
Kunze, K.L. and W.F. Trager (1993). Isoform-selective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline. Chem. Res. Toxicol. 6, 649–656.
Clarke, S.E., A.D. Ayrton, and R.J. Chenery (1994). Characterization of the inhibition of P4501A2 by furafylline. Xenobiotica 24, 517–526.
Tarrus, E., J. Cami, D.J. Roberts, R.G. Spickett, E. Celdran, and J. Segura (1987). Accumulation of caffeine in healthy volunteers treated with furafylline. Br. J. Clin. Pharmacol. 23, 9–18.
Boobis, A.R., A.M. Lynch, S. Murray, R.R. De la Torre, A. Solans, M. Farre, J. Segura et al. (1994). CYP1A2-catalyzed conversion of dietary heterocyclic amines to their proximate carcinogens is their major route of metabolism in humans. Cancer Res. 54, 89–94.
Racha, J.K., A.E. Rettie, and K.L. Kunze (1998). Mechanism-based inactivation of human cytochrome P450 1A2 by furafylline: Detection of a 1:1 adduct to protein and evidence for the formation of a novel imidazomethide intermediate. Biochemistry 37, 7407–7419.
Lewis, D.F. and B.G. Lake (1996). Molecular modelling of CYP1A subfamily members based on an alignment with CYP102: Rationalization of CYP1A substrate specificity in terms of active site amino acid residues. Xenobiotica 26, 723–753.
Lozano, J.J., E. Lopez-de-Brinas, N.B. Centeno, R. Guigo, and F. Sanz (1997). Three-dimensional modelling of human cytochrome P450 1A2 and its interaction with caffeine and MeIQ. J. Comput. Aided Mol. Des. 11, 395–408.
Nichols, W.K., D.N. Larson, and G.S. Yost (1990). Bioactivation of 3-methylindole by isolated rabbit lung cells. Toxicol. Appl. Pharmacol. 105, 264–270.
Rettie, A.E., A.W. Rettenmeier, W.N. Howald, and T.A. Baillie (1987). Cytochrome P-450-catalyzed formation of delta 4-VPA, a toxic metabolite of valproic acid. Science 235, 890–893.
Skordos, K.W., S.J. Smeal, C.A. Reilly, D.L. Lanza, and G.S. Yost (2003). Selective dehydrogenated intermediates are mechanism-based inactivators of CYP3A4, CYP2E1, and CYP2F1. In Proceedings of the 13th International Conference on Cytochromes P450. Prague, Czech Republic, p. S127.
Koop, D.R. (1990). Inhibition of ethanol-inducible cytochrome P450IIE1 by 3-amino-1,2,4-triazole. Chem. Res. Toxicol. 3, 377–383.
Voorman, R.L., S.M. Maio, N.A. Payne, Z. Zhao, K.A. Koeplinger, and X. Wang (1998). Microsomal metabolism of delavirdine: Evidence for mechanism-based inactivation of human cytochrome P450 3A4. J. Pharmacol. Exp. Ther. 287, 381–388.
Guzelian, P.S. and R.W. Swisher (1979). Degradation of cytochrome P-450 haem by carbon tetrachloride and 2-allyl-2-isopropylacetamide in rat liver in vivo and in vitro: Involvement of non-carbon monoxide-forming mechanisms. Biochem. J. 184, 481–489.
Davies, H.S., S.G. Britt, and L.R. Pohl (1986). Carbon tetrachloride and 2-isopropyl-4-pentenamide-induced inactivation of cytochrome P-450 leads to heme-derived protein adducts. Arch. Biochem. Biophys. 244, 387–352.
Osawa, Y. and L.R. Pohl (1989). Covalent bonding of the prosthetic heme to protein: A potential mechanism for the suicide inactivation or activation of hemoproteins. Chem. Res. Toxicol. 2, 131–141.
Correia, M.A., C. Decker, K. Sugiyama, P. Caldera, L. Bornheim, S.A. Wrighton et al. (1987). Degradation of rat hepatic cytochrome P-450 heme by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine to irreversibly bound protein adducts. Arch. Biochem. Biophys. 258, 436–451.
Sugiyama, K., K. Yao, A.E. Rettie, and M.A. Correia (1989). Inactivation of rat hepatic cytochrome P-450 isozymes by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine. Chem. Res. Toxicol. 2, 400–410.
Riddick, D.S. and G.S. Marks (1990). Irreversible binding of heme to microsomal protein during inactivation of cytochrome P450 by alkyl analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine. Biochem. Pharmacol. 40, 1915–1921.
Guengerich, F.P. (1978). Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase. Biochemistry 17, 3633–3639.
Guengerich, P. (1986). Covalent binding to apoprotein is a major fate of heme in a variety of reactions in which cytochrome P-450 is destroyed. Biochem. Biophys. Res. Commun. 138, 193–198.
Schaefer, W.H., T.M. Harris, and F.P. Guengerich (1985). Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P-450 heme. Biochemistry 24, 3254–3263.
Yao, K., A.M. Falick, N. Patel, and M.A. Correia (1993). Cumene hydroperoxide-mediated inactivation of cytochrome P450 2B1: Identification of an active site heme-modified peptide. J. Biol. Chem. 268, 59–65.
He, K., L.M. Bornheim, A.M. Falick, D. Maltby, H. Yin, and M.A. Correia (1998). Identification of the heme-modified peptides from cumene hydroperoxide-inactivated cytochrome P450 3A4. Biochemistry 37, 17448–17457.
Karuzina, I.I. and A.I. Archakov (1994). The oxidative inactivation of cytochrome P450 in monooxygenase reactions. Free Rad. Biol. Med. 16, 73–97.
Catalano, C.E., Y.S. Choe, and P.R. Ortiz de Montellano (1989). Reactions of the protein radical in peroxide-treated myoglobin: Formation of a hemeprotein cross-link. J. Biol. Chem. 264, 10534–10541.
Choe, Y.S. and P.R. Ortiz de Montellano (1991). Differential additions to the myoglobin prosthetic heme group. Oxidative γ-meso substitution by alkylhydrazines. J. Biol. Chem. 266, 8523–8530.
Osawa, Y., B.M. Martin, P.R. Griffin, J.R. Yates III, J. Shabanowitz, D.F. Hunt et al. (1990). Metabolism-based covalent bonding of the heme prosthetic group to its apoprotein during the reductive debromination of BrCCl3 by myoglobin. J. Biol. Chem. 265, 10340–10346.
Osawa, Y., R.J. Highet, A. Bax, and L.R. Pohl (1991). Characterization by NMR of the hememyoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring 1 vinyl group. J. Biol. Chem. 266, 3208–3214.
Kindt, J.T., A, Woods, B.M. Martin, R.J. Cotter, and Y. Osawa (1992). Covalent alteration of the prosthetic heme of human hemoglobin by BrCCl3. Cross-linking of heme to cysteine residue 93. J. Biol. Chem. 267, 8739–8743.
Docherty, J.C, G.D. Firneisz, and B.A. Schacter (1984). Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase. Arch. Biochem. Biophys. 235, 657–664.
Yoshinaga, T., S. Sassa, and A. Kappas (1982). A comparative study of heme degradation by NADPH-cytochrome C reductase alone and by the complete heme oxygenase system. Distinctive aspects of heme degradation by NADPH-cytochrome c reductase. J. Biol. Chem. 257, 7794–7802.
Cantoni, L., A.H. Gibbs, and F. De Matteis (1981). Loss of haem and haemoproteins during the generation of superoxide anion and hydrogen peroxide: A pathway not involving production of carbon monoxide. Int. J. Biochem. 13, 823–830.
Bonnett, R. and J.C.M. Stewart (1975). Photooxidation of bilirubin in hydroxylic solvents. J. Chem. Soc., Perkin Trans. 1, 224–229.
Tierney, D.J., A.L. Haas, and D.R. Koop (1992). Degradation of cytochrome P450 2E1: Selective loss after labilization of the enzyme. Arch. Biochem. Biophys. 293, 9–16.
Correia, M.A., K. Yao, S.A. Wrighton, D.J. Waxman, and A. Rettie (1992). Differential apoprotein loss of rat liver cytochromes P450 after their inactivation by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine: A case for distinct proteolytic mechanisms? Arch. Biochem. Biophys. 294, 493–503.
Correia, M.A., S.H. Davoll, S.A. Wrighton, and P.E. Thomas (1992). Degradation of rat liver cytochromes P-450 3A after their inactivation by 3,5-dicarbethyoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine: Characterization of the proteolytic system. Arch. Biochem. Biophys. 297, 228–238.
Korsmeyer, K.K., S. Davoll, M.E. Figueiredo-Pereira, and M.A. Correia (1999). Proteolytic degradation of heme-modified hepatic cytochromes P450: A role for phosphorylation, Ubiquitination and the 26S Proteasome? Arch. Biochem. Biophys. 365, 31–44.
Wang, H., M.E. Figueiredo-Pereira, and M.A. Correia (1999). CYP 3A degradation in isolated rat liver hepatocytes: 26S proteasome inhibitors as probes. Arch. Biochem. Biophys. 365, 45–53.
Correia, M.A., K. Sugiyama, and K. Yao (1989). Degradation of rat hepatic cytochrome P450p. Drug Metab. Rev. 20, 615–628.
Raner, G.M., A.D. Vaz, and M.J. Coon (1996). Metabolism of all-trans, 9-cis, and 13-cis isomers of retinal by purified isozymes of microsomal cytochrome P450 and mechanism-based inhibition of retinoid oxidation by citral. Mol. Pharmacol. 49, 515–522.
Raner, G.M., E.W. Chiang, A.D. Vaz, and M.J. Coon (1997). Mechanism-based inactivation of cytochrome P450 2B4 by aldehydes: Relationship to aldehyde deformylation via a peroxyhemiacetal intermediate. Biochemistry 36, 4895–4902.
Raner, G.M., J.A. Hatchell, M.U. Dixon, T.L. Joy, A.E. Haddy, and E.R. Johnson, (2002). Regioselective peroxo-dependent heme alkylation in P450BM3-F87G by aromatic aldehydes: Effects of alkylation on catalysis. Biochemistry 41, 9601–9610.
Kuo, C.L., G.M. Raner, A.D. Vaz, and M.J. Coon (1999). Discrete species of activated oxygen yield different cytochrome P450 heme adducts from aldehydes. Biochemistry 38, 10511–10518.
Kuo, C.L., A.D. Vaz, and M.J. Coon (1997). Metabolic activation of trans-4-hydroxy-2-nonenal, a toxic product of membrane lipid peroxidation and inhibitor of P450 cytochromes. J. Biol. Chem. 272, 22611–22616.
Ortiz de Montellano, P.R. and K.L. Kunze (1980). Inactivation of hepatic cytochrome P-450 by allenic substrates. Biochem. Biophys. Res. Commun. 94, 443–449.
Hanzlik, R.P., V. Kishore, and R. Tullman (1979). Cyclopropylamines as suicidesubstrates for cytochromes P-450. J. Med. Chem. 22, 759–761.
Macdonald, T.L., K. Zirvi, L.T. Burka, P. Peyman, and F.P. Guengerich (1982). Mechanism of cytochrome P-450 inhibition by cyclopropylamines. J. Am. Chem. Soc. 104, 2050–2052.
Ortiz de Montellano, P.R. and J.M. Mathews (1981). Inactivation of hepatic cytochrome P-450 by a 1,2,3-benzothiadiazole insecticide synergist. Biochem. Pharmacol. 30, 1138–1141.
Babu, B.R. and A.D.N. Vaz (1997). 1,2,3-Thiadiazole: A novel heterocyclic heme ligand for the design of cytochrome P450 inhibitors. Biochemistry 36, 7209–7216.
Masubuchi, Y., A. Ose, and T. Horie (2001). Diclofenac-induced inactivation of CYP3A4 and its stimulation by quinidine. Drug Metab. Dispos. 30, 1143–1148.
Shen, S., S.J. Hargus, B.M. Martin, and L.R. Pohl (1997). Cytochrome P4502C11 is a target of diclofenac covalent binding in rats. Chem. Res. Toxicol. 10, 420–423.
Chun, Y.J., S.Y. Ryu, T.C. Jeong, and M.Y. Kim (2001). Mechanism-based inhibition of human cytochrome P450 1A1 by rhapontigenin. Drug. Metab. Dispos. 29, 389–393.
Chang, T.K.H., J. Chen, and W.B.K. Lee (2001). Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: Evidence for mechanism-based inactivation of CYP1A2. J. Pharmacol. Exp. Ther. 299, 874–882.
Voorman, R.L., N.A. Payne, L.C. Wienkers, M.J. Hauer, and P.E. Sanders (2001). Interaction of delavirdine with human liver microsomal cytochrome P450: Inhibition of CYP2C9, CYP2C19, and CYP2D6. Drug Metab. Dispos. 29, 41–47.
Palamanda, J.R., C.N. Casciano, L.A. Norton, R.P. Clement, F.V. Favreau, C.C. Lin et al. (2001). Mechanism-based inactivation of CYP2D6 by 5-fluoro-2-[4-[(2-phenyl-1H-imidazol-5-yl)methyl]-1-piperazinyl]pyrimidine. Drug Metab. Dispos. 29, 863–867.
Nerland, D.E., M.M. Iba, and G.J. Mannering (1981). Use of linoleic acid hydroperoxide in the determination of absolute spectra of membrane-bound cytochrome P450. Mol. Pharmacol. 19, 162–167.
Poli, G., K. Cheeseman, T.F. Slater, and M.U. Danzani (1981). The role of lipid peroxidation in CCl4-induced damage to liver microsomal enzymes: Comparative studies in vitro using microsomes and isolated liver cells. Chem. Biol. Interact. 37, 13–24.
De Groot, H. and W. Haas (1981). Self-catalyzed O2-independent inactivation of NADPH-or dithionite-reduced microsomal cytochrome P-450 by carbon tetrachloride. Biochem. Pharmacol. 30, 2343–2347.
Fernandez, G., M.C. Villaruel, E.G.D. de Toranzo, and J.A. Castro (1982). Covalent binding of carbon to the heme moiety of cytochrome P-450 and its degradation products. Res. Commun. Chem. Pathol. Pharmacol. 35, 283–290.
De Groot, H., U. Harnisch, and T. Noll (1982). Suicidal inactivation of microsomal cytochrome P-450 by halothane under hypoxic conditions. Biochem. Biophys. Res. Commun. 107, 885–891.
Reiner, O. and H. Uehleke (1971). Bindung von Tetrachlorkohlenstoff an reduziertes mikrosomales Cytochrome P-450 und an Häm. Hoppe-Seylers Z. Physiol. Chem. 352, 1048–1052.
Cox, P.J., L.J. King, and D.V. Parke (1976). The binding of trichlorofluoromethane and other haloalkanes to cytochrome P-450 under aerobic and anaerobic conditions. Xenobiotica 6, 363–375.
Roland, W.C., D. Mansuy, W. Nastainczyk, G. Deutschmann, and V. Ullrich (1977). The reduction of polyhalogenated methanes by liver microsomal cytochrome P450. Mol. Pharmacol. 13, 698–705.
Mansuy, D. and M. Fontecave (1983). Reduction of benzyl halides by liver microsomes: Formation of 478 nm-absorbing sigma-alkyl-ferric cytochrome P-450 complexes. Biochem. Pharmacol. 32, 1871–1879.
Mansuy, D., M. Lange, J.C. Chottard, J.F. Bartoli, B. Chevrier, and R. Weiss (1978). Dichlorocarbene complexes of iron(II)-porphyrins—Crystal and molecular structure of Fe(TPP)(CCl2)(H2O). Angew. Chem. Int. Ed. Engl. 17, 781–782.
Ahr, H.J., L.J. King, W. Nastainczyk, and V. Ullrich (1980). The mechanism of chloroform and carbon monoxide formation from carbon tetrachloride by microsomal cytochrome P-450. Biochem. Pharmacol. 29, 2855–2861.
Mansuy, D., M. Lange, J.C. Chottard, and J.F. Bartoli (1978). Reaction du complexe carbenique Fe(II)(tetraphenylporphyrine)(CCl2) avec les amines primaires: Formation d’isonitriles. Tetrahedron Lett. 33, 3027–3030.
Mansuy, D. and J.-P. Battioni (1982). Isolation of sigma-alkyl-iron(III) or carbene-iron(II) complexes from reduction of polyhalogenated compounds by iron(II)-porphyrins: The particular case of halothane CF3CHClBr. J. Chem. Soc. Chem. Commun. 638–639.
Ruf, H.H., H. Ahr, W. Nastainczyk, V. Ullrich, D. Mansuy, J.-P. Battioni (1984). Formation of a ferric carbanion complex from halothane and cytochrome P-450: Electron spin resonance, electronic spectra and model complexes. Biochemistry 23, 5300–5306.
Castro, C.E., R.S. Wade, and N.O. Belser (1985). Biodehalogenation: Reactions of cytochrome P-450 with polyhalomethanes. Biochemistry 24, 204–210.
Callot, H. J. and E. Scheffer (1980). Model for the in vitro transformation of cytochrome P-450 into “green pigments.” Tetrahedron Lett. 21, 1335–1338.
Lange, M. and D. Mansuy (1981). N-Substituted porphyrin formation from carbene iron-porphyrin complexes: A possible pathway for cytochrome P-450 heme destruction. Tetrahedron Lett. 22, 2561–2564.
Chevrier, B., R. Weiss, M. Lange, J.C. Chotard, and D. Mansuy (1981). An iron(III)-porphyrin complex with a vinylidene group inserted into an iron-nitrogen bond: Relevance to the structure of the active oxygen complex of catalase. J. Am. Chem. Soc. 103, 2899–2901.
Olmstead, M.M., R.-J. Cheng, and A.L. Balch (1982). X-ray crystallographic characterization of an iron porphyrin with a vinylidene carbene inserted into an iron-nitrogen bond. Inorg. Chem. 21, 4143–4148.
Falzon, M., A. Nielsch, and M.D. Burke (1986). Denaturation of cytochrome P-450 by indomethacin and other non-steroidal anti-inflammatory drugs: Evidence for a surfactant mechanism and a selective effect of a p-chlorophenyl moiety. Biochem. Pharmacol. 35, 4019–4024.
Guengerich, F.P., G.A. Dannan, T.S. Wright, M.V. Martin, and L.S. Kaminsky (1982). Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone. Biochemistry 21, 6019–6030.
Halpert, J.R. (1995). Structural basis of selective cytochrome P450 inhibition. Annu. Rev. Pharmacol. Toxicol. 35, 29–53.
Kim, S., H. Ko, J.E. Park, S. Jung, S.K. Lee, and Y. Chun (2002). Design, synthesis, and discovery of novel trans-stilbene analogues as potent and selective human cytochrome P450 1B1 inhibitors. J. Med. Chem. 45, 160–164.
Covey, D.F. (1988). Aromatase inhibitors: Specific inhibitors of oestrogen biosynthesis. In Berg and Plempel (eds), Sterol Biosynthesis Inhibitors. Ellis Horwood Ltd., Cambridge, pp. 534–571.
Henderson, D., U.-F. Habenicht, Y. Nishino, U. Kerb, and M.F. El Etreby (1986). Aromatase inhibitors and benign prostatic hyperplasia. J. Steroid Biochem. 25, 867–876.
Van Wauwe, J.P. and P.A.J. Janssen (1989). Is there a case for P-450 inhibitors in cancer treatment. J. Med. Chem. 32, 2231–2239.
Kellis, J.T., J.J. Sheets, and L.E. Vickery (1984). Amino-steroids as inhibitors and probes of the active site of cytochrome P-450scc. Effects on the enzyme from different sources. J. Steroid Biochem. 20, 671–676.
Sheets, J.J. and L.E. Vickery (1983). Active site-directed inhibitors of cytochrome P-450scc: Structural and mechanistic implications of a side chain-substituted series of amino-steroids. J. Biol. Chem. 258, 11446–11452.
Sheets, J.J. and L.E. Vickery (1982). Proximity of the substrate binding site and the heme-iron catalytic site in cytochrome P-450scc. Proc. Natl. Acad. Sci. USA 79, 5773–5777.
Nagahisa, A., T. Foo, M. Gut, and W.H. Orme-Johnson (1985). Competitive inhibition of cytochrome P-450scc by (22R)-and (22S)-22-aminocholesterol: Side chain stereochemical requirements for C-22 amine coordination to the active-site heme. J. Biol. Chem. 260, 846–851.
Vickery, L.E. and J. Singh (1988). 22-Thio-23,24-bisnor-5-cholen-3β-ol: An active site-directed inhibitor of cytochrome P450scc. J. Steroid Biochem. 29, 539–543.
Nagahisa, A., R.W. Spencer, and W.H. Orme-Johnson (1983). Acetylenic mechanism-based inhibitors of cholesterol side chain cleavage by cytochrome P-450scc. J. Biol. Chem. 258, 6721–6723.
Olakanmi, O. and D.W. Seybert (1990). Modified acetylenic steroids as potent mechanism-based inhibitors of cytochrome P-450scc. J. Steroid Biochem. 36, 273–280.
Krueger, R.J., A. Nagahisa, M. Gut, S.R. Wilson, and W.H. Orme-Johnson (1985). Effect of P-450scc inhibitors on corticosterone production by rat adrenal cells. J. Biol. Chem. 260, 852–859.
Nagahisa, A., W.H. Orme-Johnson, and S.R. Wilson (1984). Silicon mediated suicide inhibition: An efficient mechanism-based inhibitor of cytochrome P-450scc oxidation of cholesterol. J. Am. Chem. Soc. 106, 1166–1167.
Trahanovsky, W.S. and A.L. Himstedt (1974). Oxidation of organic compounds with cerium(IV). XX. Abnormally rapid rate of oxidative cleavage of (beta-trimethylsilylethyl)-phenylmethanol. J. Am. Chem. Soc. 96, 7974–7976.
Vickery, L.E. and J. Singh (1988). 22-Thio-23,24-bisnor-5-cholen-3β-ol: An active site-directed inhibitor of cytochrome P450scc. J. Steroid Biochem. 29, 539–543.
Miao, E., C. Zuo, A. Nagahisa, B.J. Taylor, S. Joardar, C. Byon et al. (1990). Cytochrome P450scc mediated oxidation of (20S)-22-nor-22-thiacholesterol: Characterization of mechanism-based inhibition. Biochemistry 29, 2199–2204.
Brodie, A.M., H.M. Dowsett, and R.C. Coombes (1988). Aromatase inhibitors as new endocrine therapy for breast cancer. Cancer Treat. Res. 39, 51–65.
Brodie, A.M.H., P.K. Banks, S.E. Inkster, M. Dowsett, and R.C. Coombes (1990). Aromatase inhibitors and hormone-dependent cancers. J. Steroid Biochem. Mol. Biol. 37, 327–333.
Johnston, J.O. (1998). Aromatase inhibitors. Crit. Rev. Biochem. Mol. Biol. 33, 375–405.
Brodie, A., Q. Lu, and B. Long (1999). Aromatase and its inhibitors. J. Steroid Biochem. Mol. Biol. 69, 205–210.
Seralini, G. and S. Moslemi (2001). Aromatase inhibitors: Past, present and future. Mol. Cell. Endocrinol. 178, 117–131.
Recanatini, M., A. Cavalli, and P. Valenti (2002). Nonsteroidal aromatase inhibitors: Recent advances. Med. Res. Rev. 22, 282–304.
Henderson, D., U.-F. Habenicht, Y. Nishino, and M. F. El Etreby (1987). Estrogens and benign prostatic hyperplasia: The basis for aromatase inhibitor therapy. Steroids 50, 219–233.
Schweikert, H.-U. and U.W. Tunn (1987). Effects of the aromatase inhibitor testolactone on human benign prostatic hyperplasia. Steroids 50, 191–199.
Phillips, G.B., W.P. Castelli, R.D. Abbott, and P.M. McNamara (1983). Association of hyperestrogenemia and coronary heart disease in men in the Framingham cohort. Am. J. Med. 74, 863–869.
Santen, R.J., T.J. Worgul, E. Samojlik, A. Interrante, A.E. Boucher, A. Lipton et al. (1981). A randomized trial comparing surgical adrenalectomy with aminoglutethimide plus hydrocortisone in women with advanced breast cancer. Engl. J. Med. 305, 545–551.
Harris, A.L., T.J. Powles, I.E. Smith, R.C. Coombes, H.T. Ford, J.C. Gazet et al. (1983). Aminoglutethimide for the treatment of advanced postmenopausal breast cancer. Eur. J. Cancer Clin. Oncol. 19, 11–17.
Foster, A.B., M. Jarman, C.S. Leung, M.G. Rowlands, G.N. Taylor, R.G.T Plevey et al. (1985). Analogues of aminoglutethimide: Selective inhibition of aromatase. J. Med. Chem. 28, 200–204.
Foster, A.B., M. Jarman, C.-S. Leung, M.G. Rowlands, and G.N. Taylor (1983). Analogues of aminoglutethimide: Selective inhibition of cholesterol side-chain cleavage. J. Med. Chem. 26, 50–54.
Bhatnagar, A.S., A. Hausler, K. Schieweck, L.J. Browne, R. Bowman, and R.E. Steele (1990). Novel aromatase inhibitors. J. Steroid Biochem. Mol. Biol. 37, 363–367.
Lipton, A., H.A. Harvey, L.M. Demers, J.R. Hanagan, M.T. Mulagha, G.M. Kochak et al. (1990). A phase I trial of CGS 16949A: A new aromatase inhibitor. Cancer 65, 1279–1285.
Santen, R.J., L.M. Demers, H. Adlercreutz, H. Harvey, S. Santner, S. Sanders et al. (1989). Inhibition of aromatase with CGS 16949A in postmenopausal women. J. Clin. Endocrinol. Metab. 68, 99–106.
Stein, R.C., M. Dowsett, J. Davenport, A. Hedley, H.T. Ford, J.-C. Gazet et al. (1990). Preliminary study of the treatment of advanced breast cancer in postmenopausal women with the aromatase inhibitor CGS 16949A. Cancer Res. 50, 1381–1384.
Demers, L.M., J.C. Melby, T.E. Wilson, A. Lipton, H.A. Harvey, and R.J. Santen (1990). The effects of CGS 16949A, an aromatase inhibitor on adrenal mineralocorticoid biosynthesis. J. Clin. Endocrinol. Metab. 70, 1162–1166.
Tominaga, T., I. Adachi, Y. Sasaki, T. Tabei, T. Ikeda, Y. Takatsuka et al. (2003). Double-blind randomised trial comparing the non-steroidal aromatase inhibitors letrozole and fadrozole in postmenopausal women with advanced breast cancer. Ann. Oncol. 14, 62–70.
Goss, P.E. and R.E. Smith (2002). Letrozole for the management of breast cancer. Expert Rev. Anticancer. Ther. 2, 249–260.
Wouters, W., R. De Coster, R.W. Tuman, C.R. Bowden, J. Bruynseels, H. Vanderpas et al. (1989). Aromatase inhibition by R 76713: Experimental and clinical pharmacology. J. Steroid Biochem. 34, 427–430.
Wouters, W., R. De Coster, J. Van Dun, M.D.W.G. Krekels, A. Dillen, A. Raeymaekers et al. (1990). Comparative effects of the aromatase inhibitor R76713 and of its enantiomers R83839 and R83842 on steroid biosynthesis in vitro and in vivo. J. Steroid Biochem. Mol. Biol. 37, 1049–1054.
Vanden Bossche, H., G. Willemsens, I. Roels, D. Bellens, H. Moereels, M.-C. Coene et al. (1990). R 76713 and enantiomers: Selective, nonsteroidal inhibitors of the cytochrome P450-dependent oestrogen synthesis. Biochem. Pharmacol. 40, 1707–1718.
Ahmed, S., S. Adat, A. Murrells, C.P. Owen, and Y. Amanuel (2002). Design, synthesis, and evaluation of 4-(4′)-aminobenzyl)-2-oxazolidinones as novel inhibitors of the cytochrome P-450 enzyme aromatase. Bioorg. Chem. 30, 315–331.
Marchand, P., M. Le Borgne, M. Palzer, G. Le Baut, and R.W. Hartmann (2003). Preparation and pharmacological profile of 7-(alpha-Azolylbenzyl)-1H-indoles and indolines as new aromatase inhibitors. Bioorg. Med. Chem. Lett. 13, 1553–1555.
Pouget, C., C. Fagnere, J.P. Basly, G. Habrioux, and A.J. Chulia (2003). Design, synthesis and evaluation of 4-imidazolylflavans as new leads for aromatase inhibition. Bioorg. Med. Chem. Lett. 12, 2859–2861.
Buzdar, A.U. (2002). Anastrozole (Arimidex) in clinical practice versus the old ‘gold standard’, tamoxifen. Expert. Rev. Anticancer. Ther. 2, 623–629.
Wellington, K. and D.M. Faulds (2002). Anastrozole: In early breast cancer. Drugs 62, 2483–2490.
Miller, W.R., M. Stuart, T. Sahmoud, and J.M. Dixon (2002). Anastrozole (‘Arimidex’) blocks oestrogen synthesis both peripherally and within the breast in postmenopausal women with large operable breast cancer. Br. J. Cancer 87, 950–955.
Flynn, G.A., J.O. Johnston, C.L. Wright, and B.W. Metcalf (1981). The time-dependent inactivation of aromatase by 17-β-hydroxy-10-methylthioestra-1,4-dien-3-one. Biochem. Biophys. Res. Commun. 103, 913–918.
Bednarski, P.J. and S.D. Nelson (1989). Interactions of thiol-containing androgens with human placental aromatase. J. Med. Chem. 32, 203–213.
Wright, J.N., G. Slatcher, and M. Akhtar (1991). ’slow-binding’ sixth-ligand inhibitors of cytochrome P-450 aromatase. Studies with 19-thiomethyl-and 19-azido-androstenedione. Biochem. J. 273, 533–539.
Delaisi, C., B. Coucet, C. Hartmann, B. Tric, J.F. Gourvest, and D. Lesuisse (1992). RU54115, a tight-binding aromatase inhibitor potentially useful for the treatment of breast cancer. J. Steroid Biochem. Mol. Biol. 41, 773–777.
Geelen, J.A.A., G.H. Deckers, J.T.H. Van Der Wardt, H.J.J. Loozen, L.J.W. Tax, and H.J. Kloosterboer (1991). Selection of 19-(ethyldithio)-androst-4-ene-3,17-dione (ORG 30958): A potent aromatase inhibitor in vivo. J. Steroid Biochem. Mol. Biol. 38, 181–188.
Lovett, J.A., M.V. Darby, and R.E. Counsell (1984). Synthesis and evaluation of 19-aza-and 19-aminoandrostenedione analogues as potential aromatase inhibitors. J. Med. Chem. 27, 734–740.
Johnston, J.O., C.L. Wright, and B.W. Metcalf (1984). Time-dependent inhibition of aromatase in trophoblastic tumor cells in tissue culture. J. Steroid Biochem. 20, 1221–1226.
Shih, M.-J., M.H. Carrell, H.L. Carrell, C.L. Wright, J.O. Johnston, and C.H. Robinson (1987). Stereoselective inhibition of aromatase by novel epoxysteroids. J. Chem. Soc., Chem. Commun. 213–214.
Childers, W.E. and C.H. Robinson (1987). Novel 10β-thiiranyl steroids as aromatase inhibitors. J. Chem. Soc., Chem. Commun. 320–321.
Childers, W.E., J.V. Silverton, J.T. Kellis, L.E. Vickery, and C.H. Robinson (1991). Inhibition of human placental aromatase by novel homologated 19-oxiranyl and 19-thiiranyl steroids. J. Med. Chem. 34, 1344–1349.
Kellis, J.T., W.E. Childers, C.H. Robinson, and L.E. Vickery (1987). Inhibition of aromatase cytochrome P-450 by 10-oxirane and 10-thiirane substituted androgens. Implications for the structure of the active site. J. Biol. Chem. 262, 4421–4426.
Njar, V.C.O., E. Safi, J.V. Silverton, and C.H. Robinson (1993). Novel 10β-aziridinyl steroids: Inhibitors of aromatase. J. Chem. Soc. Perkin Trans. I 10, 1161–1168.
Metcalf, B.W., C.L. Wright, J.P. Burkhan, and J.O. Johnston (1981). Substrate-induced inactivation of aromatase by allenic and acetylenic steroids. J. Am. Chem. Soc. 103, 3221–3222.
Johnston, J.O. (1987). Biological characterization of 10-(2-propynyl)estr-4-ene-3,17-dione (MDL 18,962), an enzyme-activated inhibitor of aromatase. Steroids 50, 105–120.
Covey, D.G., W.F. Hood, and V.D. Parikh (1981). 10β-Propynyl-substituted steroids: Mechanism-based enzyme-activated irreversible inhibitors of estrogen biosynthesis. J. Biol. Chem. 256, 1076–1079.
Brandt, M.E., D. Puett, D.F. Covey, and S.J. Zimniski. Characterization of pregnant mare’s serum gonadotropin-stimulated rat ovarian aromatase and its inhibition by 10-propargyl-estr-4-ene-3,17-dione. J. Steroid Biochem. 34, 317–324.
Marcotte, P.A. and C.H. Robinson (1982). Synthesis and evaluation of 10-beta-substituted 4-estrene-3,17-diones as inhibitors of human placental microsomal aromatase. Steroids 39, 325–344.
Numazawa, M., A. Mutsumi, N. Asano, and Y. Ito (1993). A time-dependent inactivation of aromatase by 19-substituted androst-4-ene-3,6,17-diones. Steroids 58, 40–46.
Marcotte, P.A. and C.H. Robinson (1982). Design of mechanism-based inactivators of human placental aromatase. Cancer Res. 42, 3322–3325.
Marcotte, P.A. and C.H. Robinson (1982). Inhibition and inactivation of estrogen synthetase (aromatase) by fluorinated substrate analogues. Biochemistry 21, 2773–2778.
Numazawa, M., A. Mutsumi, K. Hoshi, M. Oshibe, E. Ishikawa, and H. Kigawa (1991). Synthesis and biochemical studies of 16-and 19-substituted androst-4-enes as aromatase inhibitors. J. Med. Chem. 34, 2496–2504.
Mann, J. and B. Pietrzak (1987). Preparation of aromatase inhibitors. Synthesis of 19,19-difluoro-4-hydroxyandrost-4-ene-3,7-dione and related compounds. J. Chem. Soc. Perkin Trans. I 385–388.
Furth, P.S. and C.H. Robinson (1989). Tritium release from [19-3H]19,19-difluoroandrost-4-ene-3,17-dione during inactivation of aromatase. Biochemistry 28, 1254–1259.
Covey, D.F. and W.F. Hood (1982). Aromatase enzyme catalysis is involved in the potent inhibition of estrogen biosynthesis caused by 4-acetoxy-and 4-hydroxy-4-androstene-3,17-dione. Mol. Pharmacol. 21, 173–180.
Brodie, A.M.H., W.M. Garrett, J.R. Hendrickson, C.-H. Tsai-Morris, P.A. Marcotte, and C.H. Robinson (1981). Inactivation of aromatase in vitro by 4-hydroxy-4-androstene-3,17-dione and 4-acetoxy-4-androstene-3,17-dione and sustained effects in vivo. Steroids 38, 693–702.
Brodie, A.M.H. (1994). Aromatase inhibitors in the treatment of breast cancer. J. Steroid. Biochem. Mol. Biol. 49, 281–287.
Di Salle, E., D. Giudici, G. Briatico, and G. Ornati (1990). Novel irreversible aromatase inhibitors. Ann. N. Y. Acad. Sci. 595, 357–367.
Di Salle, E., D. Giudici, G. Ornati, G. Briatico, R. D’Alessio, V. Villa et al. (1990). 4-Aminoandrostenedione derivatives: A novel class of irreversible aromatase inhibitors. Comparison with FCE 24304 and 4-hydroxyandrostenedione. J. Steroid Biochem. Mol. Biol. 37, 369–374.
Di Salle, E., G. Briatico, D. Giudici, G. Ornati, and T. Zaccheo (1989). Aromatase inhibition and experimental antitumor activity of FCE 24304, MDL 18962 and SH 489. J. Steroid Biochem. 34, 431–434.
Marsh, D.A., E.J. Brodie, W. Garrett, C.-H. Tsai-Morris, and A.M. Brodie (1985). Aromatase inhibitors. Synthesis and biological activity of androstenedione derivatives. J. Med. Chem. 28, 788–795.
Brodie, A.M.H., H.J. Brodie, W.M. Garrett, J.R. Hendrickson, D.H. Marsh, and C.-H. Tsai-Morris (1982). Effect of an aromatase inhibitor, 1,4,6-androstatriene-3,17-dione, on 7,12-dimethyl-[a]-anthracene-induced mammary tumors in the rat and its mechanism of action in vivo. Biochem. Pharmacol. 31, 2017–2023.
Henderson, D., G. Norbisrath, and U. Kerb (1986). 1-Methyl-1,4-androstadiene-3,17-dione (SH 489): Characterization of an irreversible inhibitor of estrogen biosynthesis. J. Steroid Biochem. 24, 303–306.
Numazawa, M., A. Mutsumi, K. Hoshi, and Y. Tanaka (1992). Androst-5-ene-7,17-dione: A novel class of suicide substrate of aromatase. Biochem. Biophys. Res. Commun. 186, 32–39.
Covey, D.F. and W.F. Hood (1981). Enzyme-generated intermediates derived from 4-androstene-3,6,17-trione and 1,4,6-androstatriene-3,17-dione cause a time-dependent decrease in human placental aromatase activity. Endocrinology 108, 1597–1599.
Numazawa, M., M. Tsuji, and A. Mutsumi (1987). Studies on aromatase inhibition with 4-androstene-3,6,17-trione: Its 3β-reduction and time-dependent irreversible binding to aromatase with human placental microsomes. J. Steroid Biochem. 28, 337–344.
Numazawa, M., K. Midzuhashi, and M. Nagaoka (1994). Metabolic aspects of the 1β-proton and the 19-methyl group of androst-4-ene-3,6,17-trione during aromatization by placental microsomes and inactivation of aromatase. Biochem. Pharmacol. 47, 717–726.
Di Salle, E., G. Ornati, D. Giudici, M. Lassus, T.R. Evans and R.C. Coombes (1992). Exemestane (FCE 24304), a new steroidal aromatase inhibitor. J. Steroid Biochem. Mol. Biol. 43, 137–143.
Geisler, J., N. King, G. Anker, G. Ornati, E. Di Salle, P.E. Lonning et al. (1998). In vivo inhibition of aromatization by exemestane, a novel irreversible aromatase inhibitor, in postmenopausal breast cancer patients. Clin. Cancer Res. 4, 2089–2093.
Clemett, D. and H.M. Lamb (2000). Exemestane: A review of its use in postmenopausal women with advanced breast cancer. Drugs 59, 1279–1296.
Brueggemeier, R.W. (2002). Overview of the pharmacology of the aromatase inactivator exemestane. Breast Cancer Res. Treat. 74, 177–185.
Dixon, J.M. (2002). Exemestane: A potent irreversible aromatase inactivator and a promising advance in breast cancer treatment. Expert Rev. Anticancer Ther. 2, 267–275.
Higa, G.M. (2002). Exemestane: Treatment of breast cancer with selective inactivation of aromatase. Am. J. Health Syst. Pharm. 59, 2194–2201.
Longcope, C., A. Femino, and J.O. Johnston (1988). Inhibition of peripheral aromatization in baboons by an enzyme-activated aromatase inhibitor (MDL 18,962). Endocrinology 122, 2007–2011.
Johnston, J.O. (1990). Studies with the steroidal aromatase inhibitor, 19-acetylenic androstenedione (MDL 18,962). J. Cancer Res. Clin. Oncol. 116, 880.
Covey, D.E., W.F. Hood, D.D. Bensen, and H.L. Carrell (1984). Hydroperoxides as inactivators of aromatase: 10-Beta-hydroperoxy-4-estrene-3,17-dione, crystal structure and inactivation characteristics. Biochemistry 23, 5398–5406.
Covey, D.F., W.F. Hood, and P.C. McMullan (1986). Studies of the inactivation of human placental aromatase by 17α-ethynyl-substituted 10β-hydroperoxy and related 19-nor steroids. Biochem. Pharmacol. 35, 1671–1674.
Bednarski, P.J., D.J. Porubek, and S.D. Nelson (1985). Thiol-containing androgens as suicide substrates of aromatase. J. Med. Chem. 28, 775–779.
Wright, J.N., van P.T. Leersum, S.G. Chamberlin and M. Akhtar (1989). Inhibition of aromatase by steroids substituted at C-19 with halogen, sulphur, and nitrogen. J. Chem. Soc. Perkin Trans. I 1647–1655.
Burkhart, J.P., N.P. Peet, C.L. Wright, and J.O. Johnston (1991). Novel time-dependent inhibitors of human placental aromatase. J. Med. Chem. 34, 1748–1750.
Numazawa, M., A. Yoshimura, M. Tachibana, M. Shelangouski, and M. Ishikawa (2002). Time-dependent aromatase inactivation by 4 beta,5 beta-epoxides of the natural substrate androstenedione and its 19-oxygenated analogs. Steroids 67, 185–193.
Vanden Bossche, H., G. Willemsens, W. Cools, P. Marichal and W. Lauwers (1983). Hypothesis on the molecular basis of the antifungal activity of N-substituted imidazoles and triazoles. Biochem. Soc. Trans. 11, 665–667.
Mercer, E.I. (1991). Sterol biosynthesis inhibitors: Their current status and modes of action. Lipids 26, 584–597.
Berg, M. and M. Plempel (eds.) (1988). Sterol Biosynthesis Inhibitors. Horwood, Ellis.
Nes, W.R. (1974). Role of sterols in membranes. Lipids 9, 596–612.
Yeagle, P.L., R.B. Martin, A.K. Lala, H.K. Lin, and K. Block (1977). Differential effects of cholesterol and lanosterol on artificial membranes. Proc. Natl. Acad. Sci. USA 74, 4924–4926.
Freter, C.E., R.C. Laderson, and D.F. Sibert (1979). Membrane phospholipid alterations in response to sterol depletion of LM cells. J. Biol. Chem. 254, 6909–6916.
Vanden Bossche, H., W. Lauwers, G. Willemsens, P. Marichal, F. Cornelissen and W. Cools (1984). Molecular basis for the antimycotic and antibacterial activity of N-substituted imidazoles and triazoles: The inhibition of isoprenoid biosynthesis. Pestic. Sci. 15, 188–198.
Heeres, J., M. De Brabander, and H. Vanden Bossche (1982). Ketoconazole: Chemistry and basis for selectivity. In P. Periti and G.G. Grossi (eds.), Current Chemotherapy and Immunotherapy, Vol. 2. American Society of Microbiology, Washington, D.C., pp. 1007–1009.
Willemsens, G., W. Cools, and H. Vanden Bossche (1980). Effects of miconazole and ketoconazole on sterol synthesis in a subcellular fraction of yeast and mammalian cells. In H. Van den Bossche (ed.), The Host-Invader Interplay Elsevier/North Holland, Amsterdam, pp. 691–694.
Murray, M., A.J. Ryan, and P.J. Little (1982). Inhibition of rat hepatic microsomal aminopyrine N-demethylase activity by benzimidazole derivatives: Quantitative structure-activity relationships. J. Med. Chem. 25, 887–892.
Santen, R.J., H. Vanden Bossche, J. Symoens, J. Brugmans, and R. DeCoster (1983). Site of action of low dose ketoconazole or androgen biosynthesis in men. J. Clin. Endocrinol. Metab. 57, 732–736.
Albengres, E., H. Le Louet, and J.P. Tillement (1998). Systemic antifungal agents. Drug interactions of clinical significance. Drug Saf. 18, 83–97.
Gahder, P., E.I. Mercer, B.C. Baldwin, and T.E. Wiggins (1983). A comparison of the potency of some fungicides as inhibitors of sterol 14-demethylation. Pest. Biochem. Physiol. 19, 1–10.
Ito, T., Y. Aoyama, K. Ishida, M. Kudoh, K. Hori, S. Tsuchiya et al. (1994). Selectivity of isoprenoid-containing imidazole antifungal compounds for sterol 14-demethylase P450 (P450(14)DM) and 7-ethoxycoumarin O-deethylase P450 of rat liver microsomes. Biochem. Pharmacol. 48, 1577–1582.
Dolle, R.E., H.S. Allaudeen, and L.I. Kruse (1990). Design and synthesis of 14α-methyl-15-aza-D-homosterols as novel antimycotics. J. Med. Chem. 33, 877–880.
Frye, L.L., K.P. Cusack, D.A. Leonard, and J.A. Anderson (1994). Oxolanosterol oximes: Dualaction inhibitors of cholesterol biosynthesis. J. Lipid Res. 35, 1333–1344.
Aoyama, Y., Y. Yoshida, Y. Sonoda, and Y. Sato (1987). 7-Oxo-24,25-dihydrolanosterol: A novel lanosterol 14α-demethylase (P-450 14DM) inhibitor which blocks electron transfer to the oxyferro intermediate. Biochim. Biophys. Acta. 922, 270–277.
Trzaskos, J.M., R.T. Fischer, S.S. Ko, R.L. Magolda, S. Stam, P. Johnson et al. (1995). Substrate-based inhibitors of lanosterol 14 alpha-methyl demethylase: II. Time-dependent enzyme inactivation by selected oxylanosterol analogs. Biochemistry 34, 9677–9681
Trzaskos, J.M., R.L. Magolda, M.F. Favata, R.T. Fischer, P.R. Johnson, H.W. Chen et al. (1993). Modulation of 3-hydroxy-3-methylglutaryl-CoA reductase by 15α-fluorolanost-7-en-3β-ol. A mechanism-based inhibitor of cholesterol biosynthesis. J. Biol. Chem. 268, 22591–22599.
Cooper, A.B., J.J. Wright, A.K. Ganguly, J. Desai, D. Loenberg, R. Parmegiani et al. (1989). Synthesis of 14-α-aminomethyl substituted lanosterol derivatives; inhibitors of fungal ergosterol biosynthesis. J. Chem. Soc., Chem. Commun. 898–900.
Frye, L.L., K.P. Cusack, and D.A. Leonard (1993). 32-Methyl-32-oxylanosterols: Dual-action inhibitors of cholesterol biosynthesis. J. Med. Chem. 36, 410–416.
Frye, L.L. and C.H. Robinson (1988). Novel inhibitors of lanosterol 14α-methyl demethylase, a critical enzyme in cholesterol biosynthesis. J. Chem. Soc. Chem. Commun. 129–131.
Mayer, R.J., J.L. Adams, M.J. Bossard, and T.A. Berkhout (1991). Effects of a novel lanosterol 14α-demethylase inhibitor on the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hep G2 cells. J. Biol. Chem. 266, 20070–20078.
Frye, L.L. and C.H. Robinson (1990). Synthesis of potential mechanism-based inactivators of lanosterol 14α-demethylase. J. Org. Chem. 55, 1579–1584.
Tuck, S.F., C.H. Robinson, and J.V. Silverton (1991). Assessment of the active-site requirements of lanosterol 14α-demethylase: Evaluation of novel substrate analogues as competitive inhibitors. J. Org. Chem. 56, 1260–1266.
Bossard, M.J., T.A. Tomaszek, T. Gallagher, B.W. Metcalf, and J.L. Adams (1991). Steroidal acetylenes: Mechanism-based inactivators of lanosterol 14α-demethylase. Bioorg. Chem. 19, 418–432.
Swinney, D.C., O.Y. So, D.M. Watson, P.W. Berry, A.S. Webb, D.J. Kertesz et al. (1994). Selective inhibition of mammalian lanosterol 14 alpha-demethylase by RS-21607 in vitro and in vivo. Biochemistry 33, 4702–4713.
Clement, O.O., C.M. Freeman, R.W. Hartmann, V.D. Handratta, T.S. Vasaitis, A.M.H. Brodie et al. (2003). Three dimensional pharmacophore modeling of human CYP17 inhibitors. Potential agents for prostate cancer therapy. J. Med. Chem. 46, 2345–2351.
Angelastro, M.R., M.E. Laughlin, G.L. Schatzman, P. Bey, and T.R. Blohm (1989). 17β-(Cyclopropylamino)-androst-5-en-3β-ol, a selective mechanism-based inhibitor of cytochrome P45017α(steroid 17α-hydroxylase/C17–20 lyase). Biochem. Biophys. Res. Commun. 162, 1571–1577.
Njar, V.C., M. Hector, and R.W. Hartmann (1996). 20-amino and 20,21-aziridinyl pregnene steroids: Development of potent inhibitors of 17 alpha-hydroxylase/C17,20-lyase (P450 17). Bioorg. Med. Chem. 4, 1447–1453.
Ling, Y.Z., J.S. Li, Y. Liu, K. Kato, G.T. Klus, and A. Brodie (1997). 17-Imidazolyl, pyrazolyl, and isoxazolyl androstene derivatives. Novel steroidal inhibitors of human cytochrome C17,20-lyase (P450(17) alpha). J. Med. Chem. 40, 3297–3304.
Jarman, M., S.E. Barrie, and J.M. Llera (1998). The 16,17-double bond is needed for irreversible inhibition of human cytochrome P45017alpha by abiraterone (17-(3-pyridyl)androsta-5, 16-dien-3beta-ol) and related steroidal inhibitors. J. Med. Chem. 41, 5375–5381.
Njar, V.C., K. Kato, I.P. Nnane, D.N. Grigoryev, B.J. Long, and A.M. Brodie (1998). Novel 17-azolyl steroids, potent inhibitors of human cytochrome 17 alpha-hydroxylase-C17,20-lyase (P450(17) alpha): Potential agents for the treatment of prostate cancer. J. Med. Chem. 41, 902–912.
Nnane, I.P., V.C. Njar, Y. Liu, Q. Lu, and A.M. Brodie (1999). Effects of novel 17-azolyl compounds on androgen synthesis in vitro and in vivo. J. Steroid Biochem. Mol. Biol. 71, 145–152.
Njar, V.C. and A.M. Brodie (1999). Inhibitors of 17alpha-hydroxylase/17,20-lyase (CYP17): Potential agents for the treatment of prostate cancer. Curr. Pharm. Des. 5, 163–180.
Zhuang, Y., B.G. Wachall, and R.W. Hartmann (2000). Novel imidazolyl and triazolyl substituted biphenyl compounds: Synthesis and evaluation as nonsteroidal inhibitors of human 17alpha-hydroxylase-C17, 20-lyase (P450 17). Bioorg. Med. Chem. 8, 1245–1252.
Long, B.J., D.N. Grigoryev, I.P. Nnane, Y. Liu, Y.Z. Ling, and A.M. Brodie (2000). Antiandrogenic effects of novel androgen synthesis inhibitors on hormone-dependent prostate cancer. Cancer Res. 60, 6630–6640.
Haidar, S., P.B. Ehmer, and R.W. Hartmann (2001). Novel steroidal pyrimidyl inhibitors of P450 17 (17 alpha-hydroxylase/C17–20-lyase). Arch. Pharm. (Weinheim) 334, 373–374.
Burkhart, J.P., P.M. Weintraub, C.A. Gates, R.J. Resvick, R.J. Vaz, D. Friedrich et al. (2002). Novel steroidal vinyl fluorides as inhibitors of steroid C17 (20) lyase. Bioorg. Med. Chem. 10, 929–934.
Clement, O.O., C.M. Freeman, R.W. Hartmann, V.D. Handratta, T.S. Vasaitis, A.M. Brodie et al. (2003). Three dimensional pharmacophore modeling of human CYP17 inhibitors. Potential agents for prostate cancer therapy. J. Med. Chem. 46, 2345–2351.
Haidar, S., P.B. Ehmer, S. Barassin, C. Batzl-Hartmann, and R.W. Hartmann (2003). Effects of novel 17alpha-hydroxylase/C17,20-lyase (P450 17, CYP 17) inhibitors on androgen biosynthesis in vitro and in vivo. J. Steroid Biochem. Mol. Biol. 84, 555–562.
Vinh, T.K., S.W. Yee, A.J. Kirby, P.J. Nicholls, and C. Simons (2001). 1-[(Benzofuran-2-yl)phenylmethyl]triazoles as steroidogenic inhibitors: Synthesis and in vitro inhibition of human placental CYP19 aromatase. Anticancer Drug Des. 16, 217–225.
Berg, A.M., A.B. Kickman, E. Miao, A. Cochran, S.R. Wilson, and W.H. Orme-Johnson (1990). Effects of inhibitors of cytochrome P-45017α on steroid production in mouse Leydig cells and mouse and pig testes microsomes. Biochemistry 29, 2193–2201.
Viger, A., S. Coustal, S. Perard, B. Chappe, and A. Marquet (1988). Synthesis and activity of new inhibitors of aldosterone biosynthesis. J. Steroid Biochem. 30, 469–472.
Viger, A., S. Coustal, S. Perard, A. Piffeteau, and A. Marquet (1989). 18-Substituted progesterone derivatives as inhibitors of aldosterone biosynthesis. J. Steroid Biochem. 33, 119–124.
Gomez-Sanchez, C.E., S. Chiou, and N. Yamakita (1993). 18-Ethynyl-deoxycorticosterone inhibition of steroid production is different in freshly isolated compared to cultured calf zona glomerulosa cells. J. Steroid Biochem. Mol. Biol. 46, 805–810.
Johnston, J.O., C.L. Wright, R.A. Bohnke, and P.R. Kastner (1991). Inhibition of aldosterone biosynthesis in primates by 18-acetylenic deoxycorticosterone. Endocrinology 128 (Suppl. Abstract 24).
Kupfer, D. (1982). Endogenous substrates of monooxygenases: Fatty acids and prostaglandins. In J.B. Schenkman and D. Kupfer (eds), Hepatic Cytochrome P450 Monooxygenase System. Pergamon Press, Elmsford, NY, pp. 157–190.
Kupfer, D. (1980). Endogenous substrates of monooxygenases: Fatty acids and prostaglandins. Pharmacol. Ther. 11, 469–496.
Hirt, D.L. and H.R. Jacobson (1991). Functional effects of cytochrome P450 arachidonate metabolites in the kidney. Semin. Nephrol. 11, 148–155.
McGiff, J.C., C.P. Quilley, and M.A. Carroll (1993). The contribution of cytochrome P450-dependent arachidonate metabolites to integrated renal function. Steroids 58, 573–579.
Harder, D.R., W.B. Campbell, and R.J. Roman (1995). Role of cytochrome P-450 enzymes and metabolites of arachidonic acid in the control of vascular tone. J. Vasc. Res. 32, 79–92.
Roman, R.J. (2002). P-450 metabolites of arachidonic acid in the control of cardiovascular function. Physiol Rev. 82, 131–185.
Hoagland, K.M., K.G. Maier, C. Moreno, M. Yu, and R.J. Roman (2001). Cytochrome P450 metabolites of arachidonic acid: Novel regulators of renal function. Nephrol. Dial. Transplant. 16, 2283–2285.
Maier, K.G. and R.J. Roman (2001). Cytochrome P450 metabolites of arachidonic acid in the control of renal function. Curr. Opin. Nephrol. Hypertens. 10, 81–87.
Roman, R.J., K.G. Maier, C.W. Sun, D.R. Harder, and M. Alonso-Galicia (2000). Renal and cardiovascular actions of 20-hydroxyeicosatetraenoic acid and epoxyeicosatrienoic acids. Clin. Exp. Pharmacol. Physiol. 27, 855–865.
Roman, R.J., M. Alonso-Galicia, and T.W. Wilson (1997). Renal P450 metabolites of arachidonic acid and the development of hypertension in Dahl salt-sensitive rats. Am. J. Hypertens. 10, 63S–67S.
Zou, A.P., Y.H. Ma, Z.H. Sui, P.R. Ortiz de Montellano, J.E. Clark, B.S. Masters et al. (1994). Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid ω-hydroxylase, on renal function in rats. J. Pharmacol. Exp. Ther. 268, 474–481.
Imig, J.D., A.P. Zou, P.R. Ortiz de Montellano, Z. Sui, and R.J. Roman (1994). Cytochrome P-450 inhibitors alter afferent arteriolar responses to elevations in pressure. Am. J. Physiol. 266, H1879–H1885.
Alkayed, N.J., E.K. Birks, A.G. Hudetz, R.J. Roman, L. Henderson, and D.R. Harder, (1996). Inhibition of brain P-450 arachidonic acid epoxygenase decreases baseline cerebral blood flow. Am. J. Physiol. 271, H1541–H1546.
Messer-Letienne, I., N. Bernard, R.J. Roman, J. Sassard, and D. Benzoni (1999). Cytochrome P-450 arachidonate metabolite inhibition improves renal function in Lyon hypertensive rats. Am. J. Hypertens. 12, 398–404.
Wang, M.H., E. Brand-Schieber, B.A. Zand, X. Nguyen, J.R. Falck, N. Balu et al. (1998). Cytochrome P450-derived arachidonic acid metabolism in the rat kidney: Characterization of selective inhibitors. J. Pharmacol. Exp. Ther. 284, 966–973.
Alonso-Galicia, M., K.G. Maier, A.S. Greene, A.W. Cowley, rJr., and R.J. Roman (2002). Role of 20-hydroxyeicosatetraenoic acid in the renal and vasoconstrictor actions of angiotensin II. Am. J. Physiol. Regul. Integr. Comp. Physiol. 283, R60–R68.
Alonso-Galicia, M., C.W. Sun, J.R. Falck, D.R. Harder, and R.J. Roman (1998). Contribution of 20-HETE to the vasodilator actions of nitric oxide in renal arteries. J. Physiol. 275, F370–F378.
Quigley, R., M. Baum, K.M. Reddy, J.C. Griener, and J.R. Falck (2000). Effects of 20-HETE and 19(S)-HETE on rabbit proximal straight tubule volume transport. Am. J. Physiol. Renal. Physiol. 278, F949–953.
Frisbee, J.C., R.J. Roman, U.M. Krishna, J.R. Falck, and J.H. Lombard (2001). Relative contributions of cyclooxygenase-and cytochrome P450 omega-hydroxylase-dependent pathways to hypoxic dilation of skeletal muscle resistance arteries. J. Vasc. Res. 38, 305–314.
Frisbee, J.C., R.J. Roman, J.R. Falck, U.M. Krishna, and J.H. Lombard (2001). 20-HETE contributes to myogenic activation of skeletal muscle resistance arteries in Brown Norway and Sprague-Dawley rats. Microcirculation 8, 45–55.
Kunert, M.P., R.J. Roman, J.R. Flack, and J.H. Lombard (2001). Differential effect of cytochrome P-450 omega-hydroxylase inhibition on O2-induced constriction of arterioles in SHR with early and established hypertension. Microcirculation 8, 435–443.
Miyata, N., K. Taniguchi, T. Seki, T. Ishimoto, M. Sato-Watanabe, Y. Yasuda et al. (2001). HET0016, a potent and selective inhibitor of 20-HETE synthesizing enzyme. Br. J. Pharmacol. 133, 325–329.
Ortiz de Montellano, P.R. and N.O. Reich (1984). Specific inactivation of hepatic fatty acid hydroxylases by acetylenic fatty acids. J. Biol. Chem. 259, 4136–4141.
CaJacob, C.A. and P.R. Ortiz de Montellano (1986). Mechanism-based in vivo inactivation of lauric acid hydroxylases. Biochemistry 25, 4705–4711.
Xu, F., W.O. Straub, W. Pak, P. Su, K.G. Maier, M. Yu et al. (2002). Antihypertensive effect of mechanism-based inhibition of renal arachidonic acid omega-hydroxylase activity. Am. J. Physiol. Regul. Integr. Comp. Physiol. 283, R710–720.
Zou, A.P., J.D. Imig, M. Kaldunski, P.R. Ortiz de Montellano, Z. Sui, and R.J. Roman (1994). Inhibition of renal vascular 20-HETE production impairs autoregulation of renal blood flow. Am. J. Physiol. 266, F275–282.
Zou, A.P., J.D. Imig, P.R. Ortiz de Montellano, Z. Sui, J.R. Falck, and R.J. Roman (1994). Effect of P-450 omega-hydroxylase metabolites of arachidonic acid on tubuloglomerular feedback. Am. J. Physiol. 266, F934–F941.
Zou, A.P., J.T. Fleming, J.R. Falck, E.R. Jacobs, D. Gebremedhin, D.R. Harder et al. (1996). 20-HETE is an endogenous inhibitor of the large-conductance Ca(2+)-activated K+ channel in renal arterioles. Am. J. Physiol. 270, R228–R237.
Stec, D.E., D.L. Mattson, and R.J. Roman (1997). Inhibition of renal outer medullary 20-HETE production produces hypertension in Lewis rats. Hypertension. 29, 315–319.
Evans, R.G., K.H. Day, R.J. Roman, K.H. Hopp, and W.P. Anderson (1998). Effects of intrarenal infusion of 17-octadecynoic acid on renal antihypertensive m echanisms in anesthetized rabbits. Am. J. Hypertens. 11, 803–812.
Sun, C.W., M. Alonso-Galicia, M.R. Taheri, J.R. Falck, D.R. Harder, and R.J. Roman (1998). Nitric oxide-20-hydroxyeicosatetraenoic acid interaction in the regulation of K+ channel activity and vascular tone in renal arterioles. Circ. Res. 83, 1069–1079.
Messer-Letienne, I., N. Bernard, R.J. Roman, J. Sassard, and D. Benzoni (1999). 20-Hydroxyeicosatetraenoic acid and renal function in Lyon hypertensive rats. Eur. J. Pharmacol. 378, 291–297.
Shak, S. I. and Goldstein (1984). Omega-oxidation is the major pathway for the catabolism of leukotriene B4 in human polymorphonuclear leukocytes. J. Biol. Chem. 259, 10181–10187.
Kikuta, Y., E. Kusunose, K. Endo, S. Yamamoto, K. Sogawa, Y. Fujii-Kuriyama et al. (1993). A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 ω-hydroxylase. J. Biol. Chem. 268, 9376–9380.
Clancy, R.M., C.A. Dahinden, and T.E. Hugli (1984). Oxidation of leukotrienes at the ω-end: Demonstration of a receptor for the 20-hydroxy derivative of leukotriene B4 on human neutrophils and implications for the analysis of leukotriene receptors. Proc. Natl. Acad. Sci. USA 81, 5729–5733.
Shak, S., N.O. Reich, I.M. Goldstein, and P.R. Ortiz de Montellano (1985). Leukotriene B4 ω-hydroxylase in human polymorphonuclear leukocytes: Suicidal inactivation by acetylenic fatty acids. J. Biol. Chem. 260, 13023–13028.
Williams, D.E., A.S. Muerhoff, N.O. Reich, C.A. CaJacob, P.R. Ortiz de Montellano, and B.S.S. Masters (1989). Prostaglandin and fatty acid ω and (ω-1) oxidation in rabbit lung. Acetylenic fatty acid mechanism based inactivators as specific inhibitors. J. Biol. Chem. 264, 749–756.
Amaral, S.L., K.G. Maier, D.N. Schippers, R.J. Roman, and A.S. Greene (2003). CYP4A metabolites of arachidonic acid and VEGF are mediators of skeletal muscle angiogenesis. Am. J. Physiol. Heart Circ. Physiol. 284, H1528–H1535.
Wang, M.H., B.A. Zand, A. Nasjletti, and M. Laniado-Schwartzman (2002). Renal 20-hydroxyeicosatetraenoic acid synthesis during pregnancy. Am. J. Physiol. Regul. Integr. Comp. Physiol. 282, R383–R389.
Nguyen, X., M.H. Wang, K.M. Reddy, J.R. Falck, and M.L. Schwartzman (1999). Kinetic profile of the rat CYP4A isoforms: Arachidonic acid metabolism and isoform-specific inhibitors. Am. J. Physiol. 276, R1691–R1700.
Brand-Schieber, E., J.F. Falck, and M. Schwartzman (2000). Selective inhibition of arachidonic acid epoxidation in vivo. J. Physiol. Pharmacol. 51, 655–672.
Fulco, A.J. (1991). P450BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation. Ann. Rev. Pharmacol. Toxicol. 31, 177–203.
Salaun, J.P., D. Reichhart, A. Simon, F. Durst, N.O. Reich, and P.R. Ortiz de Montellano (1984). Autocatalytic inactivation of plant cytochrome P-450 enzymes: Selective inactivation of the lauric acid in-chain hydroxylase from Helianthus tuberosus L. by unsaturated substrate analogs. Arch. Biochem. Biophys. 232, 1–7.
Shirane, N., Z. Sui, J.A. Peterson, and P.R. Ortiz de Montellano (1993). Cytochrome P450BM-3 (CYP102): Regiospecificity of oxidation of ω-unsaturated fatty acids and mechanism-based inactivation. Biochemistry 32, 13732–13741.
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Correia, M.A., Ortiz de Montellano, P.R. (2005). Inhibition of Cytochrome P450 Enzymes. In: Ortiz de Montellano, P.R. (eds) Cytochrome P450. Springer, Boston, MA. https://doi.org/10.1007/0-387-27447-2_7
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