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B.S. Chemistry - University of Georgia, Summa Cum Laude 2016
Research Summary: Free L-cysteine (Cys) plays a role in an array of vital processes in mammals, including the production of glutathione, as a building block in protein synthesis, and as a source for metabolites such as taurine and pyruvate. However, high levels of free cysteine are associated with rheumatoid arthritis, Parkinson’s disease, Alzheimer’s disease, and an increased risk of cardiovascular disease. Therefore, Cys levels must be tightly regulated to satisfy an organisms’ metabolic needs without causing harm. This regulation is partially performed by a mononuclear non-heme Fe(II) dependent thiol dioxygenase, cysteine dioxygenase (CDO). CDO performs the first step in cysteine catabolism by adding both oxygen atoms of molecular oxygen to the thiol group of free cysteine to produce cysteine sulfinic acid.
My research aims to elucidate how secondary coordination sphere residues affect substrate specificity and the mechanism of mammalian CDO using a variety of spectroscopic techniques, including magnetic circular dichroism (MCD), resonance Raman, electron paramagnetic resonance (EPR), and UV-vis absorption.