Mentor: Dr. Alexander Angerhofer
College of Liberal Arts and Sciences
"I have always preferred learning through experimentation to other types of learning and have a strong interest in chemistry. Attending medical school and becoming a physician has been a long-term goal. Biochemistry research is the perfect way for me to get hands-on scientific experience in a field that is both interesting and applicable to what I want to do in the future."
Microbiology and Cell Sciences
- Molecular Biology
- President's List 2014-2016
- Dean's List 2014-2016
- University Scholars Program 2016
- UF Alzheimer's Outreach Organization
- CALS Honors Program
- Florida Track Club
- UF Shands
- Brookdale Assisted Living Center
Hobbies and Interests
The Catalytic Mechanism of Oxalate Decarboxylase
Oxalate Decarboxylase from Bacillus subtilis is a Mn-dependent enzyme that exhibits a bifurcated mechanism catalyzing the degradation of oxalate to carbon dioxide and formate during 99.8% of turnover events, while during 0.2% of turnovers the enzyme acts as oxidase producing hydrogen peroxide and two equivalents of carbon dioxide. OxDC is a member of the bicupin superfamily of enzymes, with a mononuclear Mn (II) coordinated in each of its two domains. The current accepted mechanism suggest the binding of oxalate and dioxygen at the same metal center. However, recent studies suggest that oxygen could be binding at a distal location. Two tryptophan residues at the intermonomer junction suggest the idea of a long-range electron transfer. Site-directed mutants with a change in the tryptophan bridge between the Mn centers have been generated to test the catalytic relevance of this pi-stacked dimer. Formate dehydrogenase and ABTS chemical assays help examine how the change in structure affects the decarboxylase and oxidase activities, respectively, which elucidates the role of enzyme structure and long-range electron transfer between the metal centers in catalysis.