Author

Vatsala Dubey

Publication Date

1994

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Department

Department of Chemistry

LCSH

Myoglobin||Peroxides||Hydrogen-ion concentration||Organonitrogen compounds

Abstract

The reaction between metmyoglobin and para-nitroperoxybenzoic acid was studied at 0.1 M ionic strength and the apparent bimolecular rate constants were determined between pH 5.0 and 11.0. The reaction was found to be influenced by enzyme as well as substrate ionizations. Contrary to the general belief that metmyoglobin preferentially reacts with the ionized substrate, the results of this study indicate that it is the unionized substrate which is preferred. The maximal rates for the formation of Mb(IV) from the reaction of metmyoglobin and para-nitroperoxybenzoic acid were found to be higher than that for the formation of Mb(IV) from hydrogen peroxide. A model has been proposed to explain the results in which hydrogen bond formation occurs between the distal histidine and one oxygen of the substrate, facilitating O-O bond cleavage.

Comments

Includes bibliographical references (pages [44]-45)

Extent

59 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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