Noah Epstein
Structure and Properties of the Iron Sulfur Enzyme, the "Hybrid Cluster Protein"
Iron sulfur enzymes perform some of lifes most challenging chemical transformations, but how these enzymes function is largely unknown. I will be researching the structure, reactivity, and reduction/oxidation properties of a particular iron sulfur enzyme, the hybrid cluster protein (HCP), whose physiological function is unknown despite its presence in all domains of life. One goal of my research is to investigate how the structure of HCP dictates its reactivity towards a variety of substrates. A hallmark of HCP is the presence of an atypical iron-sulfur cluster (dubbed the hybrid cluster) whose structure is unique in biology. We hypothesize that this is the site of substrate binding and activation. I will determine the 3D structure of HCP by first crystallizing this protein and then determining precise atomic positions using X-ray Diffraction. I will then repeat this experiment in the presence of substrates (or with a mutated protein) to gain insight into substrate interactions with the hybrid cluster. Alongside complementary spectroscopic and electrochemical data, we aim to provide clarity to the enigmatic role of this ubiquitous enzyme.
Message to Sponsor

- Major: Chemical Biology
- Sponsor: Rose Hills Experience
- Mentor: Jonathan Rittle