Author

Aric Morgan

Publication Date

2000

Document Type

Dissertation/Thesis

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry and Biochemistry

LCSH

Peroxidase||Cytochrome c||Cytochrome oxidase||Potassium compounds||Chlorine compounds

Abstract

This thesis characterizes the reaction between K2IrCl6 and ZnCcP. This reaction was compared to previously reported data of the reaction between K2IrCl6 and two other heme proteins, metmyoglobin (metmb) and horseradish peroxidase (HRP). The reactions were monitored spectrophotometrically using diode array and stopped flow instruments. To characterize the reaction between ZnCcP and K2IrCl6, the objectives were to (1) generate the spectrum of the ZnCcP porphyrin cation radical, (2) to generate the equilibrium constant for the reaction, and (3) to generate the electron transfer rate constants. The results of the experiments showed that ZnCcP behaves differently than metmb or HRP. Previously reported data show that the reaction between K2IrCl6 and HRP and metmb have few side reactions. The reaction between ZnCcP and K2IrCl6 has a large number of side reactions. Also, the concentration of K2IrCl6 goes to zero indicating that there is no equilibrium between ZnCcP and K2IrCl6. The values for the electron transfer rate constants are about 2 s'-1 and 0.3 s'-1. The spectral data suggest that oxidation of the porphyrin ring occurs through oxidation of surface tryptophan residues.

Comments

Includes bibliographical references (pages [75]-76)

Extent

ix, 101 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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