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Mishtu Dey, PhD

Assistant Professor

Office: W285 CB
Office Phone: 319-384-1319

Lab: W276 CB

Molecular mechanisms of metalloenzymes driving important biological pathways

Research in our laboratory resides at the interface of chemistry and biology to understand the molecular mechanisms of metalloenzymes important for bioenergy conversion, human health and disease, or environmentally important. The focus is on applying spectroscopic, structural, and biochemical tools to investigate enzyme catalysis. Mammalian oxygen sensing and signaling. The cellular response to oxygen is regulated by a key transcription factor hypoxia-inducible factor (HIF) that plays an essential role in tumor angiogenesis, erythrocytosis, cell proliferation, and in the pathophysiology of ischemic disease. HIF transcriptional activity is controlled by a range of oxygen sensing and signal cascades. Defects in key oxygen sensors lead to various disease and our goal is to understand the molecular details of how these disease. Methanogenesis. Methane, the principal component of natural gas is produced biologically by a group of microbes called methanogens. Approximately one billion tons of methane is generated every year by microbial activity and serves as a valuable source of renewable energy. Methane biogenesis is catalyzed by the nickel-containing enzyme methyl coenzyme M reductase, which contains unusual amino acid modifications and we are interested in the biosynthesis of these unique post-translational modifications. Organosulfur metabolism in marine microbes. The volatile organic sulfur compound dimethylsulfide is produced in marine environments by bacterial degradation of dimethylsulfoniopropionate. About thousands of tons of dimethyl sulfide is released to the atmosphere every year and it’s acidic oxidation products initiate cloud nucleation. The pathways for this biodegradation involve enzymatic cleavage to form important metabolites that play significant role in global sulfur and carbon cycles and we are interested in investigating the mechanisms of these degrading enzymes.

PubMed link

Department/Program Affiliations:
Molecular Medicine