Erman, James E.
M.S. (Master of Science)
Department of Chemistry
Cytochrome oxidase; Hydrogen peroxide; Cytochrome c
Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c concentration (0.81-90uM) and hydrogen peroxide concentrations (0.50-200uM) at 25°C, in a 0.05M ionic strength potassium acetate/KNO^ buffer system. Eadie Hofstee plots of the initial velocity and substrate are nonlinear, holding the second substrate constant. A mechanism is proposed which includes random addition of the two substrates to the enzyme and a single catalytically active cytochrome c binding site. The mechanism includes an additional enzyme inactivation term and is consistent with prior studies on cytochrome c.peroxidase.
Henson, Danny R., "Cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide : a steady state kinetic mechanism" (1986). Graduate Research Theses & Dissertations. 2037.
vii, 50 pages
Northern Illinois University
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