Publication Date

1992

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry

LCSH

Cytochrome oxidase||Reduction (Chemistry)||Cytochromes

Abstract

The ionic strength dependence of the reduction of cytochrome c peroxidase compound I by horse cytochrome c has been studied, using stopped-flow technigue, in pH 7.5, potassium phosphate/nitrate buffer. The temperature was set at 25 ± 1° C. The wavelength was monitored at 4 32 nm, an isobestic point for ferri-/ferrocytochrome c, so only the absorbance change of the reduction of cytochrome c peroxidase compound I to compound II can be observed. The observed rate constant, kobs, as a function of the concentration of ferrocytochrome c shows a non-linear increase with increasing ionic strength. A two-parameter eguation is needed to fit the data at low ionic strength, 20 mM to 40 mM, while a three-parameter equation is needed at high ionic strength, 65 mM and above. The maximum rates of these reductions also show two different types of ionic strength dependence. At 20 mM to 40 mM ionic strength, the maximum rate of reduction decreases slightly, within experimental error, with increasing ionic strength. At high ionic strength, 65 mM to 300 mM, the reduction rate does not saturate at the highest cytochrome c concentration used. After testing different mechanisms, the simplest mechanism which can explain the data obtained at the whole ionic strength range, is a two-binding-site mechanism.

Comments

Includes bibliographical references (pages [57]-59)

Extent

viii, [70] 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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