Skip to main content
SpringerLink
Log in
Book cover

Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450 pp 299–317Cite as

Biological Diversity of Cytochrome P450 Redox Partner Systems

  • Chapter

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 851))

Abstract

Cytochrome P450 enzymes (P450s or CYPs) catalyze an enormous variety of oxidative reactions in organisms from all major domains of life. Their monooxygenase activity relies on the reductive scission of molecular oxygen (O2) bound to P450 heme iron, and thus on the delivery of two electrons to the heme iron at discrete points in the catalytic cycle. Early studies suggested that P450 redox partner machinery fell into only two major classes: either the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase, or bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. However, more recent studies, aided by genome sequence data, reveal a much more complex scenario. Several new types of P450 redox partner systems have now been characterized, including P450s naturally linked to their redox partners, or to a component protein of their P450 electron delivery system. Other P450s have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis. Further P450s are fused to non-redox partner enzymes and can catalyse consecutive reactions in a common pathway. This chapter describes the biochemistry and the enormous natural diversity of P450 redox systems, including descriptions of novel P450s fused to non-redox partner proteins.

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

References

  1. Guengerich FP, Munro AW (2013) Unusual cytochrome P450 enzymes and reactions. J Biol Chem 288:17065–17073

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  2. Rittle J, Green MT (2010) Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Science 330:933–937

    Article  CAS  PubMed  Google Scholar 

  3. Groves JT (2006) High-valent iron in chemical and biological oxidations. J Inorg Biochem 100:434–437

    Article  CAS  PubMed  Google Scholar 

  4. Pandey AV, Flück CE (2013) NADPH P450 oxidoreductase: structure, function, and pathology of diseases. Pharmacol Ther 138:229–254

    Article  CAS  PubMed  Google Scholar 

  5. Monk BC, Tomasiak TM, Keniya MV, Huschmann FU, Tyndall JD, O’Connell JD III, Cannon RD, McDonald JG, Rodriguez A, Finer-Moore JS, Stroud RM (2014) Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to the bilayer. Proc Natl Acad Sci U S A 111:3865–3870

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  6. Porter TD (1991) An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals. Trends Biochem Sci 16:154–158

    Article  CAS  PubMed  Google Scholar 

  7. Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc Natl Acad Sci U S A 94:8411–8416

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  8. Gutierrez A, Doehr O, Paine M, Wolf CR, Scrutton NS, Roberts GC (2000) Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases. Biochemistry 39:15990–15999

    Article  CAS  PubMed  Google Scholar 

  9. Gutierrez A, Munro AW, Grunau A, Wolf CR, Scrutton NS, Roberts GC (2003) Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues. Eur J Biochem 270:2612–2621

    Article  CAS  PubMed  Google Scholar 

  10. Iyanagi T, Xia C, Kim JJ (2012) NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family. Arch Biochem Biophys 528:72–89

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  11. Poulos TL, Finzel BC, Howard AJ (1987) High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195:687–700

    Article  CAS  PubMed  Google Scholar 

  12. Rheinwald JG, Chakrabarty AM, Gunsalus IC (1973) A transmissible plasmid controlling camphor oxidation in Pseudomonas putida. Proc Natl Acad Sci U S A 70:885–889

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  13. Sevrioukova IF, Garcia C, Li H, Bhaskar B, Poulos TL (2003) Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol 333:377–392

    Article  CAS  PubMed  Google Scholar 

  14. Sevrioukova IF, Poulos TL, Churbanova IY (2010) Crystal structure of the putidaredoxin reductase•putidaredoxin electron transfer complex. J Biol Chem 285:13616–13620

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  15. Churbanova IY, Poulos TL, Sevrioukova IF (2010) Production and characterization of a functional putidaredoxin reductase-putidaredoxin covalent complex. Biochemistry 49:58–67

    Article  CAS  PubMed  Google Scholar 

  16. Peterson JA, Lu JY, Geisselsoder J, Graham-Lorence S, Carmona C, Witney F, Lorence MC (1992) Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. J Biol Chem 267:14193–14203

    CAS  PubMed  Google Scholar 

  17. Bellamine A, Mangla AT, Nes WD, Waterman MR (1999) Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 96:8937–8942

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  18. McLean KJ, Warman AJ, Seward HE, Marshall KR, Girvan HM, Cheesman MR, Waterman MR, Munro AW (2006) Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions. Biochemistry 45:8427–8443

    Article  CAS  PubMed  Google Scholar 

  19. Tripathi S, Li H, Poulos TL (2013) Structural basis for effector control and redox partner recognition in cytochrome P450. Science 340:1227–1230

    Article  CAS  PubMed  Google Scholar 

  20. Green AJ, Munro AW, Cheesman MR, Reid GA, von Wachenfeldt C, Chapman SK (2003) Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI. J Inorg Biochem 93:92–99

    Article  CAS  PubMed  Google Scholar 

  21. Puchkaev AV, Ortiz de Montellano PR (2005) The Sulfolobus solfataricus electron donor partners of thermophilic CYP119: an unusual non-NAD(P)H-dependent cytochrome P450 system. Arch Biochem Biophys 434:169–177

    Article  CAS  PubMed  Google Scholar 

  22. Ricagno S, de Rosa M, Aliverti A, Zanetti G, Bolognesi M (2007) The crystal structure of FdxA, a 7Fe ferredoxin from Mycobacterium smegmatis. Biochem Biophys Res Commun 360:97–102

    Article  CAS  PubMed  Google Scholar 

  23. McLean KJ, Munro AW (2008) Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis. Drug Metab Rev 40:427–446

    Article  CAS  PubMed  Google Scholar 

  24. Ewen KM, Kleser M, Bernhardt R (2011) Adrenodoxin: the archetype of vertebrate-type [2Fe-2S] cluster ferredoxins. Biochim Biophys Acta 1814:111–125

    Article  CAS  PubMed  Google Scholar 

  25. Müller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U (2001) Adrenodoxin reductase-complex structure suggests electron transfer path in steroid biosynthesis. J Biol Chem 276:2786–2789

    Article  PubMed  Google Scholar 

  26. Hawkes DB, Slessor KE, Bernhardt PV, De Voss JJ (2010) Cloning, expression and purification of cindoxin, an unusual FMN-containing cytochrome P450 redox partner. ChemBioChem 11:1107–1114

    Article  CAS  PubMed  Google Scholar 

  27. Narhi LO, Fulco AJ (1986) Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P450 monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 261:7160–7169

    CAS  PubMed  Google Scholar 

  28. Narhi LO, Fulco AJ (1987) Identification and characterization of two functional domains in cytochrome P-450 BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 262:6683–6690

    CAS  PubMed  Google Scholar 

  29. Noble MA, Miles CS, Chapman SK, Lysek DA, Mackay AC, Reid GA, Hanzlik RP, Munro AW (1999) Roles of key active-site residues in flavocytochrome P450 BM3. Biochem J 339:371–379

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  30. Munro AW, Daff S, Coggins JR, Lindsay JG, Chapman SK (1996) Probing electron transfer in flavocytochrome P-450 BM3 and its component domains. Eur J Biochem 239:403–409

    Article  CAS  PubMed  Google Scholar 

  31. Black SD, Martin ST (1994) Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3). Biochemistry 33:12056–12062

    Article  CAS  PubMed  Google Scholar 

  32. Neeli R, Girvan HM, Lawrence A, Warren MJ, Leys D, Scrutton NS, Munro AW (2005) The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase. FEBS Lett 579:5582–5588

    Article  CAS  PubMed  Google Scholar 

  33. Kitazume T, Haines DC, Estabrook RW, Chen B, Peterson JA (2007) Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3. Biochemistry 46:11892–11901

    Article  CAS  PubMed  Google Scholar 

  34. Girvan HM, Dunford AJ, Neeli R, Ekanem IS, Waltham TN, Joyce MG, Leys D, Curtis RA, Williams P, Fisher K, Voice MW, Munro AW (2011) Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer. Arch Biochem Biophys 507:75–85

    Article  CAS  PubMed  Google Scholar 

  35. Siddhanta U, Presta A, Fan B, Wolan D, Rouseau DL, Stuehr DJ (1998) Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer. J Biol Chem 273:18950–18958

    Article  CAS  PubMed  Google Scholar 

  36. Daff SN, Chapman SK, Turner KL, Holt RA, Govindaraj S, Poulos TL, Munro AW (1997) Redox control of the catalytic cycle of flavocytochrome P-450 BM3. Biochemistry 36:13816–13823

    Article  CAS  PubMed  Google Scholar 

  37. Murataliev MB, Klein M, Fulco AJ, Feyereisen R (1997) Functional interactions in cytochrome P450 BM3: flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain. Biochemistry 36:8401–8412

    Article  CAS  PubMed  Google Scholar 

  38. Hanley SC, Ost TW, Daff S (2004) The unusual redox properties of flavocytochrome P450 BM3 flavodoxin domain. Biochem Biophys Res Commun 325:1418–1423

    Article  CAS  PubMed  Google Scholar 

  39. Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, Pessegueiro A, Fulco AJ, Cheesman MR, von Wachenfeldt C, Munro AW (2004) Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry 43:5474–5487

    Article  CAS  PubMed  Google Scholar 

  40. Chowdhary PK, Alemseghed M, Haines DC (2007) Cloning, expression and characterization of a fast self-sufficient P450: CYP102A5 from Bacillus cereus. Arch Biochem Biophys 468:32–43

    Article  CAS  PubMed  Google Scholar 

  41. Nakayama N, Takemae A, Shoun H (1996) Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum. J Biochem 119:435–440

    Article  CAS  PubMed  Google Scholar 

  42. Kitazume T, Tanaka A, Takaya N, Nakamura A, Matsuyama S, Suzuki T, Shoun H (2002) Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system. Eur J Biochem 269:2075–2082

    Article  CAS  PubMed  Google Scholar 

  43. Correll CC, Batie CJ, Ballou DP, Ludwig ML (1992) Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258:1604–1610

    Article  CAS  PubMed  Google Scholar 

  44. De Mot R, Parrey AHA (2002) A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes. Trends Microbiol 10:502–508

    Article  PubMed  Google Scholar 

  45. Warman AJ, Robinson JW, Luciakova D, Lawrence AD, Marshall KR, Warren MJ, Cheesman MR, Rigby SE, Munro AW, McLean KJ (2012) Characterization of Cupriavidus metallidurans CYP116B1 – a thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein. FEBS J 279:1675–1693

    Article  CAS  PubMed  Google Scholar 

  46. Hunter DJ, Roberts GA, Ost TW, White JH, Muller S, Turner NJ, Flitsch SL, Chapman SK (2005) Analysis of the domain properties of the novel cytochrome P450 RhF. FEBS Lett 579:2215–2220

    Article  CAS  PubMed  Google Scholar 

  47. Nagy I, Compernolle F, Ghys K, Vanderleyden J, De Mot R (1995) A single cytochrome-P-450 system is involved in degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine by Rhodococcus sp. strain ni86/21. Appl Environ Microbiol 61:2056–2060

    PubMed Central  CAS  PubMed  Google Scholar 

  48. Nagy I, Schoofs G, Compernolle F, Proost P, Vanderleyden J, De Mot R (1995) Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain ni86/21 involves an inducible cytochrome P-450 system and aldehyde dehydrogenase. J Bacteriol 177:676–687

    PubMed Central  CAS  PubMed  Google Scholar 

  49. Celik A, Roberts GA, White JH, Chapman SK, Turner NJ, Flitsch SL (2006) Probing the substrate specificity of the catalytically self-sufficient cytochrome P450RhF from a Rhodococcus sp. Chem Commun 2006:4492–4494

    Google Scholar 

  50. Liu L, Schmid RD, Urlacher VB (2006) Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319. Appl Microbiol Biotechnol 72:876–882

    Article  CAS  PubMed  Google Scholar 

  51. Liu L, Schmid RD, Urlacher VB (2010) Engineering cytochrome P450 monooxygenase CYP116B3 for high dealkylation activity. Biotechnol Lett 32:841–845

    Article  CAS  PubMed  Google Scholar 

  52. Coelho PS, Wang ZJ, Ener ME, Baril SA, Kannan A, Arnold FH, Brustad EM (2013) A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat Chem Biol 9:485–487

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  53. Butler CF, Peet C, Mason AE, Voice MW, Leys D, Munro AW (2013) Key mutations alter the cytochrome P450 BM3 conformational landscape and remove inherent substrate bias. J Biol Chem 288:25387–25399

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  54. Sabbadin F, Grogan G, Bruce NC (2013) LICRED: a versatile drop-in vector for rapid generation of redox-self-sufficient cytochromes P450. Methods Mol Biol 987:239–249

    CAS  PubMed  Google Scholar 

  55. Seth-Smith HM, Rosser SJ, Basran A, Travis ER, Dabbs ER, Nicklin S, Bruce NC (2002) Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous. Appl Environ Microbiol 68:4764–4771

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  56. Jackson RG, Rylott EL, Fournier D, Hawari J, Bruce NC (2007) Exploring the biochemical properties and remediation applications of the unusual explosive-degrading P450 system XplA/B. Proc Natl Acad Sci U S A 104:16822–16827

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  57. Rylott EL, Jackson RG, Sabbadin F, Seth-Smith HM, Edwards J, Chong CS, Strand SE, Grogan G, Bruce NC (2011) The explosive-degrading cytochrome P450 XplA: biochemistry, structural features and prospects for bioremediation. Biochim Biophys Acta 1814:230–236

    Article  CAS  PubMed  Google Scholar 

  58. Sabbadin F, Jackson R, Haider K, Tampi G, Turkenburg JP, Hart S, Bruce NC, Grogan G (2009) The 1.5-Å structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive. J Biol Chem 284:28467–28475

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  59. Raag R, Martinis SA, Sligar SG, Poulos TL (1991) Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala. Biochemistry 30:11420–11429

    Article  CAS  PubMed  Google Scholar 

  60. Bui SH, McLean KJ, Cheesman MR, Bradley JM, Rigby SE, Levy CW, Leys D, Munro AW (2012) Unusual spectroscopic and ligand binding properties of the cytochrome P450-flavodoxin fusion enzyme XplA. J Biol Chem 287:19699–19714

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  61. McCarthy AA, Walsh MA, Verma CS, O’Connell DP, Reinhold M, Yalloway GN, D’Arcy D, Higgins TM, Voordouw G, Mayhew SG (2002) Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris. Biochemistry 41:10950–10962

    Article  CAS  PubMed  Google Scholar 

  62. Seth-Smith HM, Edwards J, Rosser SJ, Rathbone DA, Bruce NC (2008) The explosive-degrading cytochrome P450 system is highly conserved among strains of Rhodococcus spp. Appl Environ Microbiol 74:4550–4552

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  63. Jackson CJ, Lamb DC, Marczylo TH, Warrilow AG, Manning NJ, Lowe DJ, Kelly DE, Kelly SL (2002) A novel sterol 14α-demethylase/ferredoxin fusion protein from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J Biol Chem 277:46959–46965

    Article  CAS  PubMed  Google Scholar 

  64. Geer LY, Domrachev M, Lipman DJ, Bryant SH (2002) CDART: protein homology by domain architecture. Genome Res 12:1619–1623

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  65. Tsitsigiannis DI, Kowieski TM, Zarnowski R, Keller NP (2005) Three putative oxylipin biosynthetic genes integrate sexual and asexual development in Aspergillus nidulans. Microbiology 151:1809–1821

    Article  CAS  PubMed  Google Scholar 

  66. Tsitsigiannis DI, Keller NP (2006) Oxylipins act as determinants of natural product biosynthesis and seed colonization in Aspergillus nidulans. Mol Microbiol 59:882–892

    Article  CAS  PubMed  Google Scholar 

  67. Brodhun F, Gobel C, Hornung E, Feussner I (2009) Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450. J Biol Chem 284:11792–11805

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  68. Brodhun F, Schneider S, Gobel C, Hornung E, Feussner I (2010) PpoC from Aspergillus nidulans is a fusion protein with only one active haem. Biochem J 425:553–565

    Article  CAS  PubMed  Google Scholar 

  69. Hansen BG, Mnich E, Nielsen KF, Nielsen JB, Nielsen MT, Mortensen UH, Larsen TO, Patil KR (2012) Involvement of a natural fusion of a cytochrome P450 and a hydrolase in mycophenolic acid biosynthesis. Appl Environ Microbiol 78:4908–4913

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  70. Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y (2003) Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis − crystallographic, spectroscopic, and mutational studies. J Biol Chem 278:9761–9767

    Article  CAS  PubMed  Google Scholar 

  71. Fujishiro T, Shoji O, Nagano S, Sugimoto H, Shiro Y, Watanabe Y (2011) Crystal structure of H2O2-dependent cytochrome P450SPα with its bound fatty acid substrate: insight into the regioselective hydroxylation of fatty acids at the α position. J Biol Chem 286:29941–29950

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  72. Matsunaga I, Sumimoto T, Ueda A, Kusunose E, Ichihara K (2000) Fatty acid-specific, regiospecific, and stereospecific hydroxylation by cytochrome P450 (CYP152B1) from Sphingomonas paucimobilis: substrate structure required for α-hydroxylation. Lipids 35:365–371

    Article  CAS  PubMed  Google Scholar 

  73. Matsunaga I, Yokotani N, Gotoh O, Kusunose E, Yamada M, Ichihara K (1997) Molecular cloning and expression of fatty acid α-hydroxylase from Sphingomonas paucimobilis. J Biol Chem 272:23592–23596

    Article  CAS  PubMed  Google Scholar 

  74. Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K (1999) Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450. Lipids 34:841–846

    Article  CAS  PubMed  Google Scholar 

  75. Rude MA, Baron TS, Brubaker S, Alibhai M, Del Cardayre SB, Schirmer A (2011) Terminal olefin (1-alkene) biosynthesis by a novel P450 fatty acid decarboxylase from Jeotgalicoccus species. Appl Environ Microbiol 77:1718–1727

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  76. Belcher J, McLean KJ, Matthews S, Woodward LS, Fisher K, Rigby SE, Nelson DR, Potts D, Baynham MT, Parker DA, Leys D, Munro AW (2014) Structure and biochemical properties of the alkene producing cytochrome P450 OleT JE (CYP152L1) from the Jeotgalicoccus sp. 8456 bacterium. J Biol Chem 289:6535–6550

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  77. Girhard M, Schuster S, Dietrich M, Dürre P, Urlacher VB (2007) Cytochrome P450 monooxygenase from Clostridium acetobutylicum: a new α-fatty acid hydroxylase. Biochem Biophys Res Commun 362:114–119

    Article  CAS  PubMed  Google Scholar 

  78. Liu Y, Wang C, Yan J, Zhang W, Guan W, Lu X, Li S (2014) Hydrogen peroxide-independent production of α-alkenes by OleT JE P450 fatty acid decarboxylase. Biotechnol Biofuels 7:28

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  79. Daiber A, Shoun H, Ullrich V (2005) Nitric oxide reductase (P450nor) from Fusarium oxysporum. J Inorg Biochem 99:185–193

    Article  CAS  PubMed  Google Scholar 

  80. Shoun H, Tanimoto T (1991) Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J Biol Chem 266:11078–11082

    CAS  PubMed  Google Scholar 

  81. Usuda K, Toritsuka N, Matsuo Y, Kim DH, Shoun H (1995) Denitrification by the fungus Cylindrocarpon tonkinense: anaerobic cell growth and two isozyme forms of cytochrome P-450nor. Appl Environ Microbiol 61:883–889

    PubMed Central  CAS  PubMed  Google Scholar 

  82. Shoun H, Fushinobu S, Jiang L, Kim SW, Wakagi T (2012) Fungal denitrification and nitric oxide reductase cytochrome P450nor. Phil Trans R Soc B Biol Sci 367:1186–1194

    Article  CAS  Google Scholar 

  83. Shiro Y, Fujii M, Iizuka T, Adachi S, Tsukamoto K, Nakahara K, Shoun H (1995) Spectroscopic and kinetic-studies on reaction of cytochrome P450nor with nitric oxide − implication for its nitric oxide reduction mechanism. J Biol Chem 270:1617–1623

    Article  CAS  PubMed  Google Scholar 

  84. Lehnert N, Praneeth VKK, Paulat F (2006) Electronic structure of iron(II)-porphyrin nitroxyl complexes: molecular mechanism of fungal nitric oxide reductase (P450nor). J Comput Chem 27:1338–1351

    Article  CAS  PubMed  Google Scholar 

  85. Kostanjevecki V, Leys D, Van Driessche G, Meyer TE, Cusanovich MA, Fischer U, Guisez Y, Van Beeumen J (1999) Structure and characterization of Ectothiorhodospira vacuolata cytochrome b 558, a prokaryotic homologue of cytochrome b 5. J Biol Chem 274:35614–35620

    Article  CAS  PubMed  Google Scholar 

  86. Altuve A, Silchenko S, Lee KH, Kuczera K, Terzyan S, Zhang X, Benson DR, Rivera M (2001) Probing the differences between rat liver outer mitochondrial membrane cytochrome b 5 and microsomal cytochromes b 5. Biochemistry 40:9469–9483

    Article  CAS  PubMed  Google Scholar 

  87. Spatz L, Strittmatter P (1973) A form of reduced nicotinamide adenine dinucleotide cytochrome b 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment. J Biol Chem 248:793–799

    CAS  PubMed  Google Scholar 

  88. Guzov VM, Houston HL, Murataliev MB, Walker FA, Feyereisen R (1996) Molecular cloning, overexpression in Escherichia coli, structural and functional characterization of house fly cytochrome b 5. J Biol Chem 271:26637–26645

    Article  CAS  PubMed  Google Scholar 

  89. Funk WD, Lo TP, Mauk MR, Brayer GD, MacGillivray RT, Mauk AG (1990) Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b 5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7. Biochemistry 29:5500–5508

    Article  CAS  PubMed  Google Scholar 

  90. Hildebrandt A, Estabrook RW (1971) Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions. Arch Biochem Biophys 143:66–79

    Article  CAS  PubMed  Google Scholar 

  91. Correia MA, Mannering GJ (1973) Reduced diphosphopyridine nucleotide synergism of the reduced triphosphopyridine nucleotide-dependent mixed-function oxidase system of hepatic microsomes. II. Role of the type I drug-binding site of cytochrome P-450. Mol Pharmacol 9:470–485

    CAS  PubMed  Google Scholar 

  92. Sang-Choul I, Waskell L (2011) The interaction of microsomal cytochrome P450 2B4 with its redox partners, cytochrome P450 reductase and cytochrome b 5. Arch Biochem Biophys 507:144–153

    Article  CAS  Google Scholar 

  93. Katagiri M, Kagawa N, Waterman MR (1995) The role of cytochrome b 5 in the biosynthesis of androgens by human P450C17. Arch Biochem Biophys 317:343–347

    Article  CAS  PubMed  Google Scholar 

  94. Akhtar M, Wright JN, Lee-Robichaud P (2011) A review of mechanistic studies on aromatase (CYP19) and 17α-hydroxylase-17,20-lyase (CYP17). J Steroid Biochem Mol Biol 125:2–12

    Article  CAS  PubMed  Google Scholar 

  95. Storbeck KH, Swart AC, Goosen P, Swart P (2013) Cytochrome b 5: novel roles in steroidogenesis. Mol Cell Endocrinol 371:87–99

    Article  CAS  PubMed  Google Scholar 

  96. Finn RD, McLaughlin LA, Ronseaux S, Rosewell I, Houston JB, Henderson CJ, Wolf CR (2008) Defining the in vivo role for cytochrome b 5 in cytochrome P450 function through the conditional hepatic deletion of microsomal cytochrome b 5. J Biol Chem 283:31385–31393

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  97. McLaughlin LA, Ronseaux S, Finn RD, Henderson CJ, Wolf CR (2010) Deletion of microsomal cytochrome b 5 profoundly affects hepatic and extrahepatic drug metabolism. Mol Pharmacol 78:269–278

    Article  CAS  PubMed  Google Scholar 

  98. Ichinose H, Wariishi H (2012) Heterologous expression and mechanistic investigation of a fungal cytochrome P450 (CYP5150A2): involvement of alternative redox partners. Arch Biochem Biophys 518:8–15

    Article  CAS  PubMed  Google Scholar 

  99. Syed K, Kattamuri C, Thompson TB, Yadav JS (2011) Cytochrome b 5 reductase-cytochrome b 5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: atypical properties and in vivo evidence of electron transfer capability to CYP63A2. Arch Biochem Biophys 509:26–32

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  100. Henderson CJ, McLaughlin LA, Wolf CR (2013) Evidence that cytochrome b 5 and cytochrome b 5 reductase can act as sole electron donor to the hepatic cytochrome P450 system. Mol Pharmacol 83:1209–1217

    Article  CAS  PubMed  Google Scholar 

  101. Noble MA, Girvan HM, Smith SJ, Smith WE, Murataliev M, Guzov VM, Feyereisen R, Munro AW (2007) Analysis of the interactions of cytochrome b 5 with flavocytochrome P450 BM3 and its domains. Drug Metab Rev 39:599–617

    Article  CAS  PubMed  Google Scholar 

  102. Nelson DR, Goldstone JV, Stegeman JJ (2013) The cytochrome P450 genesis locus: the origin and evolution of animal cytochrome P450s. Philos Trans R Soc Lond B Biol Sci 368(1612):20120474

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  103. Munro AW, Girvan HM, McLean KJ (2007) Variations on a (t)heme − novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily. Nat Prod Rep 24:585–609

    Article  CAS  PubMed  Google Scholar 

  104. Sadeghi SJ, Gilardi G (2013) Chimeric P450 enzymes: activity of artificial redox fusions driven by different reductases for biotechnological applications. Biotechnol Appl Biochem 60:102–110

    Article  CAS  PubMed  Google Scholar 

  105. Munro AW, Girvan HM, McLean KJ (2007) Cytochrome P450 – redox partner fusion enzymes. Biochim Biophys Acta 1770:345–359

    Article  CAS  PubMed  Google Scholar 

  106. Hamdane D, Xia C, Im SC, Zhang H, Kim JJ, Waskell L (2009) Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450. J Biol Chem 284:11374–11378

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  107. Filenko N, Spiro S, Browning DF, Squire D, Overton TW, Cole J, Constantinidou C (2007) The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase. J Bacteriol 189:4410–4417

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  108. Macedo S, Mitchell EP, RomÐo CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P (2002) Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 Å resolution using synchrotron radiation. J Biol Inorg Chem 7:514–525

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK

    Kirsty J. McLean, Dominika Luciakova, James Belcher, Kang Lan Tee & Andrew W. Munro

Authors
  1. Kirsty J. McLean
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Dominika Luciakova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. James Belcher
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Kang Lan Tee
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Andrew W. Munro
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Andrew W. Munro .

Editor information

Editors and Affiliations

  1. Faculty of Pharmaceutical Sciences, The University of British Columbia, Vancouver, British Columbia, Canada

    Eugene G. Hrycay

  2. Fac. of Pharmaceutical Sciences, The University of British Columbia , Vancouver, British Columbia, Canada

    Stelvio M. Bandiera

Rights and permissions

Reprints and permissions

Copyright information

© 2015 Springer International Publishing Switzerland

About this chapter

Cite this chapter

McLean, K.J., Luciakova, D., Belcher, J., Tee, K.L., Munro, A.W. (2015). Biological Diversity of Cytochrome P450 Redox Partner Systems. In: Hrycay, E., Bandiera, S. (eds) Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450. Advances in Experimental Medicine and Biology, vol 851. Springer, Cham. https://doi.org/10.1007/978-3-319-16009-2_11

Download citation

Publish with us

Policies and ethics

Search

Navigation