Dmitri Davydov

  1. Research Professor
Email Addressd.davydov@wsu.edu
LocationFulmer 410

Biography

Education

Research Fellow (“poste verte”, biophysics), 1991-1993, Institut de Biologie Physico-Chimique, INSERM Unité 310, Paris, France

Ph. D. in Biochemistry, 1987, Russian State Medical University (former N.I. Pirogov 2-nd Moscow Medical Institute), Moscow, Russia

M.S. in Biochemistry, 1978, M. V. Lomonosov Moscow State University, Moscow, Russia

Dmitri R. Davydov is an enzymologist and biophysicist with over 40 years of experience in molecular enzymology, protein biophysics, and high-pressure bioscience.  His research is  directed towards understanding the mechanisms of protein–protein and enzyme–substrate interactions in cytochromes P450 and exploring protein conformational dynamics related to the mechanisms of their function and regulation. In his current research, Dr. Davydov focuses on the systems biochemistry of drug metabolism and the mechanisms of functional integration in the human cytochrome P450 ensemble.

Publications

  • Davydov, D.R., Davydova, N.Y., Rodgers, J.T., Rushmore, T.H., and Jones, J.P.(2017) Toward a systems approach to the human cytochrome P450 ensemble: interactions between CYP2D6 and CYP2E1 and their functional consequences. Biochem. J. 474, 3523-3542
  • Rodgers, J.T., Davydova, N.Y., Paragas, E.M., Jones, J.P., and Davydov, D.R. (2018) Kinetic mechanism of time-dependent inhibition of CYP2D6 by 3,4-methylenedioxymethamphetamine (MDMA): Functional heterogeneity of the enzyme and the reversibility of its inactivation. Biochem. Pharm., 156, 86-98
  • Davydova, N. Y., Dangi, B., Maldonado, M. A., Vavilov, N. E., Zgoda, V. G., and Davydov, D. R. (2019) Toward a systems approach to cytochrome P450 ensemble: interactions of CYP2E1 with other P450 species and their impact on CYP1A2, Biochem J. 476, 3661-3685.
  • Gerringer ME, Yancey PH, Tikhonova OV, Vavilov NE, Zgoda VG, Davydov DR. (2020) Pressure tolerance of deep-sea enzymes can be evolved through increasing volume changes in protein transitions: a study with lactate dehydrogenases from abyssal and hadal fishes. FEBS J., 287, 5394-5410
  • Zhang B, Lewis KM, Abril A, Davydov DR, Vermerris W, Sattler SE, Kang C. (2020). Structure and Function of the Cytochrome P450 Monooxygenase, Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor. Plant Physiology, 183, 957-973
  • Dangi, B., Davydova, N.Y., Vavilov, N.E., Zgoda, V.G. and Davydov, D.R. (2020) Nonadditivity in Human Microsomal Drug-Metabolizing Ensemble Revealed with Coumarin-152, a Polyspecific Cytochrome P450  Substrate, Xenobiotica, 50, 1393-1405
  • Dangi, B., Davydova, N. Y., Maldonado, M.A., Abbasi, A., Vavilov, N. E., Zgoda, V. G. and Davydov, D. R. (2021) Effects of alcohol-induced increase in CYP2E1 content in human liver microsomes on the activity and cooperativity of CYP3A4, Arch. Biochem. Biophys., 698, 108677
  • Dangi, B., Davydova, N. Y., Maldonado, M. A., Ahire, D., Prasad, B., and Davydov, D. R. (2021) Probing functional interactions between cytochromes P450 with principal component analysis of substrate saturation profiles and targeted proteomics, Arch Biochem Biophys 708, 108937
  • Davydov, D.R., Prasad B. (2021) Assembling the P450 puzzle: on the sources of nonadditivity in drug metabolism, Trends Pharm Sci 42, 988-997
  • Davydov, D. R., Dangi, B., Yue, G., Ahire, D. S., Prasad, B., and Zgoda, V. G. (2022) Exploring the Interactome of Cytochrome P450 2E1 in Human Liver Microsomes with Chemical Crosslinking Mass Spectrometry, MDPI Biomolecules 12, 185
  • Zhang, B.X.; Kang, C.; Davydov, D.R. (2022) Conformational Rearrangements in the Redox Cycling of NADPH-Cytochrome P450 Reductase from Sorghum bicolor Explored with FRET and Pressure-Perturbation Spectroscopy. MDPI Biology 2022, 11,
  • Zhang, B.X.; Munske, G.R.; Timokhin, V.I.; Ralph, J.; Davydov, D.R.; Vermerris, W.; Sattler, S.E.; Kang, C. (2022) Functional and structural insight into the flexibility of cytochrome P450 reductases from Sorghum bicolor and its implications for lignin composition. J. Biol. Chem. 2022, 298