Denis A. Proshlyakov
- B.S. 1989, Pirogov Moscow State Medical University, Moscow, Russia
- M.S. 1992, Pirogov Moscow State Medical University, Moscow, Russia
- Ph.D. 1995, Graduate University for Advanced Studies, Yokohama, Japan
proshlya@msu.edu
22A Chemistry Building
Michigan State University
East Lansing, MI 48824-1322
Phone: 517-355-9715 x260
Fax: 517-353-1793
Proshlyakov Lab Page
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Denis A. Proshlyakov
Research Interests
About one third of
all enzymes are metalloenzymes, which incorporate functionally important and
often redox-active metal ion(s). Cytochromes P450, peroxodases, cyclooxygenases,
lipoxygensaes, all components of respiratory chain, and nitric oxide synthases
– are only few examples of metalloenzymes, which control a vast range of
critical biological functions. A particularly prominent subgroup of metalloenzymes
uses either heme cofactors or non-heme mono- and di-nuclear iron and copper centers.
These enzymes are brilliantly tuned to balance a difficult task of harvesting
strong oxidizing power of oxygen for specific biological chemistry without release
of toxic active oxygen.
Research in my laboratory focuses on the uncovering sub-molecular mechanisms of
action of metalloenzymes. We utilize a broad range of techniques—optical,
vibrational and magnetic resonance spectroscopies in combination with isotope
substitution, electrochemistry, surface immobilization, photolysis etc.—
to gain insight into individual reaction steps. Currently our interest is focused
on iron-oxygen chemistry catalyzed by both heme-based and non-heme iron enzymes. We are interested in similarities and differences between these two large classes of enzymes, including control over highly reactive and toxic transient oxygen species and the rationale for development of heme systems in higher organisms. Heme-based catalytic enzymes are beautifully represented by dioxygen reduction by heme-copper terminal oxidases,
which sustain electron flow through respiratory chain of aerobes by reducing
molecular oxygen to water in their binuclear catalytic center. One of the better studied examples of the second class is a bacterial dioxygenase TauD, which utilizes
a non-heme, mononuclear iron ion to activate molecular oxygen and catalyzes alpha-ketoglutarate-dependent release of sulfite
from taurine.
Recent Publications
Dai Y, Proshlyakov DA, Zak JK, Swain GM. "Optically transparent diamond electrode for use in ir transmission spectroelectrochemical measurements." Anal Chem. 79(19):7526-33 (2007)
Proshlyakov, D.A., Henshaw, T.F., Monterosso, G.R., Ryle, M.J., Hausinger, R.P., “Direct detection of oxygen intermediates in the non-heme Fe enzyme Taurine\a-ketoglutarate Dioxygenase” J. Am. Chem. Soc. 126 (4) 1022-1023 (2004)
Proshlyakov, D.A. “UV optical absorption by protein radicals in cytochrome c oxidase” Biochim. Biophys. Acta 1655(1-3) 282-289 (2004)
Egawa, T., Proshlyakov, D. A., Miki, H., Makino, R., Ogura, T., Kitagawa, T., Ishimura, Y., “Effects of a thiolate axial ligand on the p → p* electronic states of oxoferryl porphyrins: a study of the optical and resonance Raman spectra of compounds I and II of chloroperoxidase” J. Biol. Inorg. Chem. 6(1) 46-54 (2001)
Proshlyakov, D. A., Pressler, M. A., DeMaso, C., Leykam, J. F., DeWitt, D. L., Babcock, G. T., “Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244” Science 290(5496) 1588-1591 (2000)
Hoganson, C. W., Pressler, M. A., Proshlyakov, D. A., Babcock, G. T., “From water to oxygen and back again: mechanistic similarities in the enzymatic redox conversions between water and dioxygen,” Biochim. Biophys. Acta 1365(1-2) 170-174 (1998)