Project Description
Molybdenum containing enzymes are found throughout nature playing key roles in the global carbon, nitrogen, and sulfur cycles. The diverse chemistry of this family of enzymes is facilitated by the molybdenum cofactor and the protein environment the cofactor is found, but little in known about how the cofactor and peptide environment poise the enzyme for the specific catalytic outcomes. The focus of this project is to characterize formate dehydrogenase and expand on our recent work that demonstrates the enzyme can be tuned for different catalytic outcomes. Recently, work in my group identified a variant of formate dehydrogenase that changes the native activity and imbues a new function to the enzyme. The goal of this support will be to facilitate the training and research progress for the student. Specifically, the student will be trained in protein expression and purification, and kinetic characterization of the enzyme and variants with the goal of understanding the role of the residues that have been changed in the variant.
Tasks and Responsibilites
The student will work with a senior graduate student and the PI to first learn the critical techniques required for advanced characterization of the enzyme. The student will express the enzyme in E. coli and purify it learning important techniques that can be applied in future work whether in graduate school or industrial applications. Following purification, the student will cary out kinetic assays to characterize the enzyme under various conditions (pH, inhibitors, etc) so we will better understand how the variant has changed the intrinsic reactivity of the enzyme. As with protein purification, these skills are broadly applicable across academic research or industry, setting the student up for future successes after leaving UWM.
Desired Qualifications
None listed.