Erman, James E.
M.S. (Master of Science)
Department of Chemistry
Oxidation; Hydrogen peroxide; Oxidases; Cytochrome c
Initial velocities for the cytochrome c peroxidase- catalyzed oxidation of ferrocytochrome c by hydrogen peroxidase have been measured as a function of both hydrogen peroxide concentrations (0.2 5-200.0μM) and ferrocytochrome c concentrations (0.5-105.0μM) in 0.01M potassium phosphate, pH 7.5 with the ionic strength adjusted to 0.05M with KNO₃ at 25°C. For each substrate, Hanes-Woolf plots of the initial velocity and substrate are linear, holding the second substrate constant. A steady state mechanism which includes random addition of the two substrates to the enzyme, rapid equilibration for the binding of cytochrome c at a single binding site on cytochrome c peroxidase, and irreversible redox steps is sufficient to account for the kinetic data. The rate and equilibrium constants evaluated from the steady state data agree well with independent measurements reported in the literature.
Kim, Kil Lyong, "The cytochrome C peroxidase-catalyzed oxidation of ferrocytochrome C by hydrogen peroxide" (1983). Graduate Research Theses & Dissertations. 5395.
vi, 34 pages
Northern Illinois University
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