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Assistant Professor of Chemistry
Office: W285 CBIowa City, IA 52242
Email: firstname.lastname@example.orgWeb: More About Dr. Dey - Related Websites and Resources
MS, Utkal UniversityPhD, Indian Institute of Technology Bombay
Post Doctorate, University of Michigan-Ann Arbor & University of Nebraska-LincolnPost Doctorate, Massachusetts Institite of Technology
Interdisciplinary Graduate Program in Molecular and Cellular Biology
"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 valuable. The focus is on applying X-ray crystallographic, spectroscopic, and biochemical tools to investigate enzyme catalysis.
Biological methane formation and naturally occurring amino acid modifications. 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 unique amino acid modifications near the active site. Our goal is to investigate the biosynthesis of these rare post-translational modifications.
Organosulfur metabolism in marine microbes. The volatile organic sulfur compound dimethylsulfide (DMS) is produced in marine environments by bacterial degradation of dimethylsulfoniopropionate (DMSP). About thousands of tons of DMS is released to the atmosphere every year and it’s acidic oxidation products initiate cloud nucleation. The pathways for DMSP degradation involve enzymatic cleavage to simpler sulfur compounds that are important metabolites for marine bacteria and play significant role in global sulfur and carbon cycles. We are interested in investigating the mechanisms of DMSP degrading enzymes in marine bacteria.
Metalloproteins in mammalian oxygen sensing pathway. The response to oxygen in mammals is regulated by hypoxia-inducible factor (HIF), a key transcription factor that senses oxygen. Under normal oxygen conditions, iron enzymes hydroxylate HIF and promote degradation. With limiting oxygen, hydroxylation of HIF is diminished thereby stimulating the transcription of hypoxia target genes. Defects in crucial oxygen sensing proteins will result in defects in erythropoiesis, angiogenesis, cell proliferation, and apoptosis. Our focus is directed towards understanding various aspects of mammalian oxygen sensing at a molecular level."
Center for Biocatalysis and Bioprocessing
Date Last Modified: 10/09/2015 -
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