Publication Date

1989

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry

LCSH

Cytochromes||Chemical kinetics||Oxidation

Abstract

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.

Comments

Includes bibliographical references (pages 49-51)

Extent

vii, 51 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

Share

COinS