about
Compressibility of the heme pocket of substrate analogue complexes of cytochrome P-450cam-CO. The effect of hydrostatic pressure on the Soret band.Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET)Allosteric transitions in cytochrome P450eryF explored with pressure-perturbation spectroscopy, lifetime FRET, and a novel fluorescent substrate, Fluorol-7GA.The role of cytochrome P450 2B6 and 2B4 substrate access channel residues predicted based on crystal structures of the amlodipine complexesMultiple substrate-binding sites are retained in cytochrome P450 3A4 mutants with decreased cooperativity.Concurrent cooperativity and substrate inhibition in the epoxidation of carbamazepine by cytochrome P450 3A4 active site mutants inspired by molecular dynamics simulations.Interactions among cytochromes P450 in microsomal membranes: oligomerization of cytochromes P450 3A4, 3A5, and 2E1 and its functional consequencesA large-scale allosteric transition in cytochrome P450 3A4 revealed by luminescence resonance energy transfer (LRET).Mechanisms that regulate production of reactive oxygen species by cytochrome P450.Pivotal role of P450-P450 interactions in CYP3A4 allostery: the case of α-naphthoflavone.Microsomal monooxygenase as a multienzyme system: the role of P450-P450 interactions.Effect of glutathione on homo- and heterotropic cooperativity in cytochrome P450 3A4.CYP261 enzymes from deep sea bacteria: a clue to conformational heterogeneity in cytochromes P450.Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein.Role of subunit interactions in P450 oligomers in the loss of homotropic cooperativity in the cytochrome P450 3A4 mutant L211F/D214E/F304W.Cytochrome P450 from Photobacterium profundum SS9, a piezophilic bacterium, exhibits a tightened control of water access to the active siteAllosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket.Mechanism of interactions of alpha-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe.Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization.Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum.Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: the effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium.Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy.Role of cytochrome B5 in modulating peroxide-supported cyp3a4 activity: evidence for a conformational transition and cytochrome P450 heterogeneity.High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: evidence for conformational inhomogeneity in the oligomers.Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy.Comparative study of monomeric reconstituted and membrane microsomal monooxygenase systems of the rabbit liver. II. Kinetic parameters of reductase and monooxygenase reactionsHigh pressure induced inactivation of ferrous cytochrome P-450 LM2 (IIB4) CO complex: evidence for the presence of two conformers in the oligomerReduction and catalytic properties of cytochrome P-450 LM2 in reconstituted system containing monomeric carriersRandom distribution of NADPH-specific flavoprotein and cytochrome P-450 in liver microsomesInteractions of cytochrome P450 2B4 with NADPH-cytochrome P450 reductase studied by fluorescent probeDynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4Allosteric P450 mechanisms: multiple binding sites, multiple conformers or both?Variable path length and counter-flow continuous variation methods for the study of the formation of high-affinity complexes by absorbance spectroscopy. An application to the studies of substrate binding in cytochrome P450
P50
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P50
description
researcher ORCID ID = 0000-0001-8520-0033
@en
wetenschapper
@nl
name
Dmitri R Davydov
@ast
Dmitri R Davydov
@en
Dmitri R Davydov
@nl
type
label
Dmitri R Davydov
@ast
Dmitri R Davydov
@en
Dmitri R Davydov
@nl
prefLabel
Dmitri R Davydov
@ast
Dmitri R Davydov
@en
Dmitri R Davydov
@nl
P108
P106
P108
P31
P496
0000-0001-8520-0033