Date of Award

Spring 2006

Degree Type

Thesis - Restricted

Degree Name

Master of Science (MS)

Department

Chemistry

First Advisor

Kincaid, James

Second Advisor

Reid, S. A.

Third Advisor

Sem, Daniel

Abstract

Heme proteins are a well-studied class of enzymes capable of varied catalytic function. Some of the best known heme proteins are hemoglobin and myoglobin, oxygen carrying and storing proteins respectively, which are found in all vertebrate circulatory systems. The oxygen binding and releasing parameters of these proteins, as well as possible cooperativity between the four subunits of hemoglobin, have been studied extensively. Another facet of heme chemistry is the ability of these proteins to form high valent peroxo and hydroperoxo species after reduction of the oxygenated molecules, protonation of the distal oxygen atom, and fast scission of the oxygen-oxygen bond. These proposed intermediates are just now being characterized by Resonance Raman Spectroscopy, an ideal technique to use owing to its power to selectively enhance the vibrational modes of the heme prosthetic group. This allows for attention to be focused on the active site of hemoglobin while avoiding complications due to spectral bands arising from the rest of the protein. In this work, Co (II) substituted hemoglobin was prepared and irradiated by 6° Co ')'-rays at 77 K, with the intention to both induce radiolytic reduction to peroxo and hydroperoxo species and characterize them by Resonance Raman Spectroscopy. Meso/Proto Hemoglobin hybrids and Co/Fe Hemoglobin hybrids were also prepared for use in collaborative studies performed at another university.

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