D
Dmitri R. Davydov
Researcher at Washington State University
Publications - 64
Citations - 2386
Dmitri R. Davydov is an academic researcher from Washington State University. The author has contributed to research in topics: Cooperativity & Hydrostatic pressure. The author has an hindex of 28, co-authored 62 publications receiving 2217 citations. Previous affiliations of Dmitri R. Davydov include University of California, San Diego & University of Texas Southwestern Medical Center.
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Journal ArticleDOI
Mechanisms that regulate production of reactive oxygen species by cytochrome P450.
TL;DR: An overview of recent advances in understanding of feedback mechanisms that serve to limit P450 production of ROS is provided, including those that affect physiological and cellular effects of P450 generation of ROS.
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Allosteric P450 mechanisms: multiple binding sites, multiple conformers or both?
TL;DR: Application of the concept of an oligomeric allosteric enzyme to microsomal cytochromes P450 in combination with a general paradigm of multiple ligand occupancy of the active site provides an excellent explanation for complex manifestations of the atypical kinetic behavior of the enzyme.
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High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers
Dmitri R. Davydov,Eric Deprez,Gaston Hui Bon Hoa,Tatiana V. Knyushko,G P Kuznetsova,Yakov M. Koen,Alexander I. Archakov +6 more
TL;DR: Analysis of the pressure-induced spin shift versus benzphetamine concentration shows this transition to be caused mainly by changes in the spin equilibrium of both substrate-bound and substrate-free hemoprotein, whereas the substrate binding step itself has a very weak pressure dependency.
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Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization.
TL;DR: Results suggest that in CYP3A4 oligomers in solution and in the membrane the enzyme is distributed between two persistent conformers with different accessibility of the heme for the reductant (SO*-(2) anion monomer).
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Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy.
TL;DR: The results suggest that both in solution and in the membrane CYP3A4 is represented by two conformers with different positions of spin equilibrium and different barotropic properties, which suggests unusual stabilization of the high-spin state of CYP4, which is assumed to reflect decreased water accessibility of the heme moiety due to specific interactions of the hemoprotein with the protein partners and/or membrane lipids.