Abstract
Abstract Steady-State and transient-state kinetic studies of the cytochrome c peroxidase (CcP) catalyzed oxidation of ferrocytochrome c by hydrogen peroxide at pH 7.5 as a function on ionic strength have been carried out using both horse heart and yeast iso-1 cytochrome c. The ionic strength affects the apparent interaction between cytochrome c and the oxidized intermediates of CcP while the intracomplex electron transfer rates are essentially independent of ionic strength. The maximum enzyme turnover rates for the oxidation of yeast iso-1 and horse heart ferrocytochrome c are 780 ± 130 s−1 and 280 ± 40 s−1, respectively, independent of ionic strength at pH 7.5. The intramolecular electron transfer rates from bound ferrocytochrome c to the heme site in CcP compound I is about 1900 s−1 and 450 s−1 for yeast iso-1 and horse heart cytochrome c, respectively.
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