Resonance Raman Studies of the Cyanide Adducts of Cytochrome c Peroxidase

Author

Cynthia Rajani, Marquette University

Date of Award

Fall 1994

Document 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 coordinating a cyanide ligand 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 ligand binding. These structural features may mimic those which occur when the enzyme binds its natural substrate H₂0₂.

Recommended Citation

Rajani, Cynthia, "Resonance Raman Studies of the Cyanide Adducts of Cytochrome c Peroxidase" (1994). Master's Theses (1922-2009) Access restricted to Marquette Campus. 2654.
https://epublications.marquette.edu/theses/2654