Mentor: Professor Sharon Burgmeyer
A common motif of biochemistry is the role metals play as cofactors in the active sites of enzymes. Molybdenum enzymes are found throughout biology, and fulfill important tasks such as nitrogen metabolism in plants. All molybdenum enzymes employ this metal in the same way in the form of Moco, the molybdenum cofactor. The most important piece of this complicated cofactor is a single molybdenum atom with two important components, or ligands. This unique constituent is incorporated into every molybdenum enzyme, and is known as the molybdopterin ligand.
This special piece of the molybdenum cofactor controls its reactivity, and begins to explain the bioinorganic chemistry of Mo enzymes. For this reason, the study of the electronics, spectroscopy, and mechanisms of this molecule is a topic of great interest in our research.
This summer, I will be performing reactions to synthesize molybdenum compounds that are substituted with this crucial ligand to further my understanding of their oxidation-reduction chemistry. Generally, this reaction has the following setup:
Pterinyl Alkyne + Tp*Mo(O)(S4) → Tp*Mo(O)(S2Alkyne)
Rebecca Petit and I will be studying variants of this reaction and the synthesis and analytical techniques required for their success. Throughout the summer we hope to achieve a better understanding of molybdopterin chemistry by investigating the effects of varying substituent groups (labeled R in the above figure) on this portion of the molybdenum cofactor.