Date of Award

Fall 1996

Degree Type

Thesis - Restricted

Degree Name

Master of Science (MS)

Department

Chemistry

Abstract

lactoperoxidase is an enzyme that catalyzes the oxidation of a variety of organic and inorganic substrates in secretory fluids of mammals. Most notably, it catalyzes the peroxidation of endogenous thiocyanate (SCN-) ion to the antimicrobial hypothiocyanate (OSCN-). It is classified as a peroxidase by the International Union of Pure and Applied Chemistry's Enzyme Commission, but is more commonly known as a heme protein. Heme proteins have a prosthetic metallomacrocyclic structure, known as heme, bound to the apoprotein matrix via an amino acid side chain to the iron cation center at the 5th coordination site. The biomolecular environment on the opposing side of the molecule is the site for catalysis. Elucidation of the enzymatic mechanisms and the heme environment can be probed with resonance Raman spectroscopy. Aided by multiple spectroscopic techniques, resonance Raman spectroscopy can be a valuable tool in ascertaining structure-function relationships of biomolecules such as heme proteins like lactoperoxidase.

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