Publication Date

1981

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Legacy Department

Department of Chemistry

LCSH

Imidazole; Chemical bonds; Hydrogen-ion concentration; Myoglobin

Abstract

4-Nitroimidazole binding to horse heart metmyoglobin was studied as a function of pH and ionic strength. The pKa of 4- nitroimidazole was also studied as a function of ionic strength. It appears that two ionizable groups on the protein affect the observed association rate constant within the pH range of 5 to 11. The alkaline group, which has a pKa of 8.9, is responsible for the acid-alkaline transition of the protein. The more acidic group has a pKa near 6. This group only appears to influence the binding of 4-nitroimidazole at high ionic strengths. The ionic strength dependence of the rate constants does not indicate whether the neutral or anionic form of the ligand is preferentially bound to metmyoglobin. It is concluded that both forms of the ligand may contribute to the observed association rate constant.

Comments

Includes bibliographical references.||Includes illustrations.

Extent

vi, 60 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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