1. The kinetics of ferrocytochrome c peroxidation by yeast peroxidase are described. Kinetic differences between the older and more recent preparations of the enzyme most probably arise from differences in intrinsic turnover rates. 2. The time-courses of cytochrome c peroxidation by the enzyme follow essentially first-order kinetics in phosphate buffer. Deviations from first-order kinetics occur in acetate buffer, and are due to a higher enzymic turnover rate in this medium accompanied by a greater tendency to autocatalytic peroxidation of cytochrome c. 3. The kinetics of ferrocytochrome c peroxidation by yeast peroxidase are interpreted in terms of a mechanism postulating formation of reversible complexes between the peroxidase and both reduced and oxidized cytochrome c. Formation of these complexes is inhibited at high ionic strengths and by polycations. 4. Oxidized cytochrome c can act as a competitive inhibitor of ferrocytochrome c peroxidation by peroxidase. The Ki for ferricytochrome c is approximately equal to the Km for ferrocytochrome c and thus probably accounts for the observed apparent first-order kinetics even at saturating concentrations of ferrocytochrome c. 5. The results are discussed in terms of a possible analogy between the oxidations of cytochrome c catalysed by yeast peroxidase and by mammalian cytochrome oxidase.
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Research Article|
January 01 1971
Complex-formation between cytochrome c and cytochrome c peroxidase. Kinetic studies
Peter Nicholls;
Peter Nicholls
1Department of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K., and State University of New York at Buffalo, Buffalo, N.Y. 14214, U.S.A.
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Eugene Mochan
Eugene Mochan
1Department of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K., and State University of New York at Buffalo, Buffalo, N.Y. 14214, U.S.A.
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Publisher: Portland Press Ltd
© 1971 The Biochemical Society
1971
Biochem J (1971) 121 (1): 55–67.
Citation
Peter Nicholls, Eugene Mochan; Complex-formation between cytochrome c and cytochrome c peroxidase. Kinetic studies. Biochem J 1 January 1971; 121 (1): 55–67. doi: https://doi.org/10.1042/bj1210055
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