Publication Date

1986

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Legacy Department

Department of Chemistry

LCSH

Cytochrome oxidase; Hydrogen peroxide; Cytochrome c

Abstract

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.

Comments

Bibliography: pages [49]-50.

Extent

vii, 50 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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