Date of Award

Fall 1994

Degree Type

Thesis - Restricted

Degree Name

Master of Science (MS)

Department

Chemistry

Abstract

The active site of the enzyme cytochrome c peroxidase is a combination of its prosthetic group, protoheme b, and certain key protein residues located both proximally and distally to the heme group. By coordinatinq a cyanide liqand to the sixth coordination position of the heme iron(III) molecule, a relatively stable species can be produced. Resonance Raman spectroscopy can then be used to study the effect of the active site environment upon liqand bindinq. These structural features may mimic those which occur when the enzyme binds its natural substrate H202.

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