Author

Kil Lyong Kim

Publication Date

1983

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry

LCSH

Oxidation||Hydrogen peroxide||Oxidases||Cytochrome c

Abstract

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.

Comments

Bibliography : leaf [34].

Extent

vi, 34 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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