Erman, James E.
M.S. (Master of Science)
Department of Chemistry
Cytochromes; Chemical kinetics; Oxidation
The steady state kinetics of the oxidation of ferrocytochrome c to ferricytochrome c by cytochrome c peroxidase are being studied as a function of viscosity. The viscosity of the reaction medium is being altered using sucrose, over the range of 0% sucrose to 55% sucrose by weight. The apparent bimolecular rate constants are determined at each of the sucrose concentrations, and are found to be independent of viscosity. The apparent bimolecular rate constant determined is (2.96 ± .382) X 10⁷ M⁻¹s⁻¹. This is two orders of magnitude below a typical diffusion controlled reaction rate constant of 10⁹ M⁻¹s⁻¹. The conclusion drawn is that the oxidation of ferrocytochrome c by cytochrome c peroxidase is not diffusion controlled.
Brown, Michael E., "A steady state kinetic study of the oxidation of ferrocytochrome C to ferricytochrome C by cytochrome C peroxidase as a function of viscosity" (1989). Graduate Research Theses & Dissertations. 574.
vii, 51 pages
Northern Illinois University
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