Research in our laboratory resides at the interface of chemistry and biology to understand the molecular mechanisms of enzymes important for bioenergy conversion, human health and disease, or environmentally valuable. We use a combination of enzymology, microbiology, molecular biology, biophysical methods, including X-ray crystallography to investigate structure-function relationship. Our research is highly interdisciplinary, drawing from synthetic chemistry, protein biochemistry, biophysics, and microbial bioprocessing.
Proline hydroxylation and 2-oxoglutarate dioxygenases. Proline hydroxylation is an essential post-translational modification occurring in all organisms. Hydroxylation of proline is catalyzed by mononuclear non-heme iron 2-oxoglutarate-dependent prolyl-hydroxylases. These enzymes regulate diverse biological processes and are involved in a variety of diseases. We are investigating the regulatory mechanisms of some of these prolyl-hydroxylases.
Metallocofactors and Microbial Sulfur Cycle. The organic sulfur compound dimethylsulfoniopropionate (DMSP) is a key nutrient in marine environments and is a major precursor for the climate-active gas dimethylsulfide (DMS). DMS plays a major role in the biogeochemical cycling of sulfur. We employ mechanistic and structural enzymology tools to address fundamental questions related to DMSP and DMS cycling from marine milieus.
Enzyme Regulation and Metabolism. Using biophysical and structural approaches, we investigate the regulation mechanism of enzyme involved in key metabolic pathway.