Summary
Five oxidation states of horseradish peroxidase, ferrous, ferric, Compounds I and II, oxy-ferrous, are known. Various reactions and plausible structures of these states are reported. Mechanisms of peroxidase-oxidase reactions are discussed in terms of the five oxidation states of the enzyme.
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References
W. M. Latimer, Oxidation Potentials, Second Edition. Prentice-Hall, Inc., Englewood Cliffs, 1952.
I. Yamazaki, R. Nakajima, K. Miyoshi, R. Makino and M. Tamura, Oxidases and Related Redox Systems (T. E. King, H. S. Mason and M. Morrison, eds.), University park press, in press, (1973).
L. M. Shannon, E. Kay and J. Y. Lew. J. Biol. Chem., 241, 2166 (1966).
K. G. Paul, Acta Chem. Scand., 12, 1312 (1958).
Y. Sawada, T. Ohyama and I. Yamazaki, Biochim. Biophys. Acta, 268, 305 (1972).
Y. Saito and M. Mochizuki, Proc. Intern. Conf. Med. Electron. Biol. Eng., p. 600, Tokyo (1965).
T. Nakamura, J. Japan. Biochem. Soc., 39, 855 (1967).
H. Theorell, Enzymologia, 10, 250 (1942).
H. Theorell, Arkiv Kemi Mineral. Geol., A 16, No 3 (1942).
P. George, Nature, 169, 612 (1952).
P. George, Biochem. J., 54, 267 (1953).
B. Chance, Arch. Biochem. Biophys., 41, 416 (1952).
I. Yamazaki, H. S. Mason and L. H. Piette, J. Biol. Chem., 235, 2444 (1960).
I. Yamazaki and L. H. Piette, Biochim. Biophys. Acta, 50, 62 (1961).
F. Björkstén, Biochim. Biophys. Acta, 212, 396 (1970).
R. Roman and H. B. Dunford, Biochemistry, 11, 2076 (1972).
K. Miyoshi and I. Yamazaki, Enzyme Communications, in press.
I. Yamazaki, Advan. in Biophys. (Tokyo), 2, 33 (1971).
B. Swedin and H. Theorell, Nature, 145, 71 (1940).
B. Chance, J. Biol. Chem. 197, 577 (1952).
R. H. Kenten, Biochem. J., 59, 110 (1955).
I. Yamazaki, K. Fujinaga, I. Takehara and H. Takahashi, J. Biochem., 43, 377 (1956).
T. Akazawa and E. E. Conn, J. Biol. Chem., 232, 403 (1958).
M. H. Klapper and D. P. Hackett, J. Biol. Chem., 238, 3736 (1963).
I. Yamazaki, Proc. Intern. Symp. on Enzyme Chem., Tokyo and Kyoto (1957), p. 224. Maruzen, Tokyo (1958).
I. Yamazaki and L. H. Piette, Biochim. Biophys. Acta, 77, 47 (1963).
T. Odajima, Biochim. Biophys. Acta, 235, 52 (1971).
H. Yamazaki and I. Yamazaki, Arch. Biochem. Biophys. 154, 147 (1973).
J. M. McCord and I. Fridovich, J. Biol. Chem., 244, 6049 (1969).
G. Rotilis, R. C. Bray and M. Fielden, Biochim. Biophys. Acta, 268, 605 (1972).
Y. Sawada and I. Yamazaki, to be published.
T. Odajima and I. Yamazaki, Biochim. Biophys. Acta, 284, 355 (1972).
R. W. Miller and E. V. Parpus, Arch. Biochem. Biophys. 143, 276 (1971).
G. A. Maclachlan and E. R. Waygood, Can. J. Biochem. Physiol., 34, 1233 (1956).
I. Yamazaki and H. Souzu, Arch. Biochem. Biophys. 86, 294 (1960).
P. M. Ray, Arch. Biochem. Biophys. 87, 10 (1960).
R. M. Ray, Arch. Biochem. Biophys. 96, 199 (1962).
R. L. Himan and L. Lang, Biochemistry 4, 144 (1965).
L. R. Fox, W. K. Purves and H. I. Nakada, Biochemistry 4, 2754 (1965).
J. Ricard and J. Nari, Biochim. Biophys. Acta, 113, 57 (1966).
J. Ricard and J. Nari, Biochim. Biophys. Acta, 132, 321 (1967).
P. M. Ray and K. V. Thimann, Arch. Biochem. Biophys. 64, 175 (1956).
Y. Morita, K. Kameda and M. Mizuno, Agr. Biol. Chem. (Tokyo), 26, 442 (1962).
Y. Morita, Y. Kominato and K. Shimizu, Mem. Res. Inst. Food Sci. Kyoto Univ., 28, 1 (1967).
H. A. Harbury, J. Biol. Chem., 225, 1009 (1957).
H. Theorell, Adv. Enzymol. 7, 265 (1947).
R. Lemberg and J. W. Legge, Hematin Compounds and Bile Pigments, p. 348 Interscience Publishers Inc., New York (1949).
H. S. Mason, Avd. Enzymol., 19, 79 (1957).
H. S. Mason, Proc. Intern. Symp. Enzyme Chem., Tokyo and Kyoto (1957), p. 220, Maruzen, Tokyo (1958).
M. H. Klapper and D. P. Hackett, J. Biol. Chem., 238, 3743 (1963).
K. Yokota and I. Yamazaki, Biochim. Biophys. Acta, 105, 301 (1965).
M. Shin, K. Tagawa and D. I. Arnon, Biochem. Z., 338, 84 (1963).
H. Lundegårdh, Nature, 181, 28 (1958).
H. Theorell, Arkiv kemi Mineral. Geol., 14 B, No 20 (1940).
I. Yamazaki, R. Nakajima, H. Honma and M. Tamura, Biochem. Biophys. Res. Commun., 27, 53 (1967).
Y. Morita and K. Kameda, Mem. Res. Inst. Food Sci., Kyoto Univ., 12, 1 (1957).
R. Nakajima and I. Yamazaki, unpublished observation.
B. Hagihara, K. Tagawa, I. Morikawa, M. Shin and K. Okunuki, Nature, 181, 1656 (1958).
Y. Morita, Mem. Res. Inst. Food Sci., Kyoto Univ., 11, 38 (1956).
R. Nakajima, H. Sano and I. Yamazaki, Biochim. Biophys. Acta, 172, 578 (1969).
D. Keilin and T. Mann, Proc. Roy. Soc. London, Series B, 122, 119 (1937).
P. George, J. Biol. Chem., 201, 427 (1953).
I. Yamazaki, K. Yokota and R. Nakajima, Oxidases Related Redox Systems (T. E. King, H. S. Mason and M. Morrison, eds.) p. 485. John Wiley, New York, (1965).
B. Chance, Oxidases and Related Redox Systems (T. E. King, H. S. Mason and M. Morrison, eds.) p. 504. John Wiley, New York (1965).
I. Yamazaki and K. Yokota, Biochem. Biophys. Res. Commun., 19, 249 (1965).
I. Yamazaki, K. Yokota and M. Tamura, Hemes and Hemoproteins (B. Chance, R. E. Estabrook, T. Yonetani, eds.) p. 319. Academic Press, New York, (1966).
J. B. Wittenberg, R. W. Noble, B. A. Wittenberg, E. Antonini, M. Brunori and J. Wyman, J. Biol. Chem., 242, 626 (1967).
I. Yamazaki, H. Yamazaki, M. Tamura, T. Ohnishi, S. Nakamura and T. Iyanagi, Advances in Chemistry Series, 77-III, 290 (1968).
M. Tamura and I. Yamazaki, J. Biochem., 71, 311 (1972).
K. Yokota and I. Yamazaki, Biochem. Biophys. Res. Commun., 18, 48 (1965).
S. Nakamura and I. Yamazaki, Biochim. Biophys. Acta, 189, 29 (1969).
R. Lemberg, Reviews of Pure and Applied Chemistry, 6, 1 (1956).
I. Yamazaki, H. Sano, R. Nakajima and K. Yokota, Biochem. Biophys. Res. Commun., 31, 932 (1968).
B. Chance, Arch. Biochem., 21, 416 (1949).
H. Yamazaki, S. Ohishi and I. Yamazaki, Arch. Biochem. Biophys., 136, 41 (1970).
I. Yamazaki and K. Yokota, Biochim. Biophys. Acta, 132, 310 (1967).
E. J. Land and A. J. Swallow, Biochim. Biophys. Acta, 234, 34 (1971).
K. Yokota and I. Yamazaki, to be published.
H. Degn, Biochim. Biophys. Acta, 180, 271 (1969).
H. Degn, Biochim. Biophys. Acta, 180, 291 (1969).
A. Lotka, J. Phys. Chem., 14, 271 (1910).
P. Nicholls, J. Gen. Physiol., 49, 131 (1965).
A. F. W. Coulson and T. Yonetani, Biochem. Biophys. Res. Commun., 49, 391 (1972).
R. Makino and I. Yamazaki, J. Biochem., 72, 655 (1972).
R. Makino and I. Yamazaki, Arch. Biochem. Biophys., in press.
M. Tamura, T. Asakura and T. Yonetani, Biochim. Biophys. Acta, 268, 292 (1972).
A. S. Brill and R. J. P. Williams, Biochem. J., 78, 246 (1961).
J. Peisach, W. E. Blumberg, B. A. Wittenberg and J. B. Wittenberg, J. Biol. Chem., 243, 1871 (1968).
Y. Maeda and Y. Morita, Biochem. Biophys. Res. Commun., 29, 680 (1967).
T. H. Moss, A. Ehrenberg and A. J. Bearden, Biochemistry, 8, 4159 (1969).
D. Dolphin, A. Forman, D. C. Borg, J. Fajer and R. H. Felton, Proc. Nat. Acad. Sci., 68, 614 (1971).
G. R. Schonbaum and S. Lo, J. Biol. Chem., 247, 3353 (1972).
H. Theorell and A. Ehrenberg, Arch. Biochem. Biophys., 41, 442 (1952).
P. George, Arch. Biochem. Biophys., 45, 21 (1953).
P. George, J. Biol. Chem., 201, 413 (1953).
R. R. Fergusson, J. Am. Chem. Soc., 78, 741 (1956).
T. Yonetani, H. Schleyer and A. Ehrenberg, J. Biol. Chem., 241, 3240 (1966).
J. Peisach, private communication.
P. George and D. H. Irvine, Biochem. J., 52, 511 (1952).
N. K. King and M. E. Winfield, J. Biol. Chem., 238, 1520 (1963).
T. Yonetani and H. Schleyer, J. Biol. Chem., 242, 1974 (1967).
A. F. W. Coulson, J. E. Erman and T. Yonetani, J. Biol. Chem., 246. 917 (1971).
R. W. Noble and Q. H. Gibson, J. Biol. Chem., 245, 2409 (1970).
B. Chance and J. Higgins, Arch. Biochem., 22, 224 (1949).
B. Chance and R. R. Fergusson, The Mechanism of Enzyme Action (W. D. McElroy and B. Glass, eds.), p. 389, Johns Hopkins Univ. Press, Baltimore (1954).
M. J. Comier and P. M. Pricard, J. Biol. Chem., 243, 4706 (1968).
B. B. Hashinoff and H. B. Dunford, Biochemistry 9, 4930 (1970).
R. Roman, H. B. Dunford and M. Evett, Can. J. Chem., 49, 3059 (1971).
B. Chance, Adv. Enzymol., 12, 153 (1951).
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Yamazaki, I., Yokota, Kn. Oxidation states of peroxidase. Mol Cell Biochem 2, 39–52 (1973). https://doi.org/10.1007/BF01738677
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DOI: https://doi.org/10.1007/BF01738677