Date of Award
Thesis - Restricted
Master of Science (MS)
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.
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.