Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering.
about
Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductaseSubstrate-specific modulation of CYP3A4 activity by genetic variants of cytochrome P450 oxidoreductaseThe molecular biology, biochemistry, and physiology of human steroidogenesis and its disordersThe syndrome of 17,20 lyase deficiencyConformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor BindingThe crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3Molecular view of an electron transfer process essential for iron-sulfur protein biogenesisStructural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenaseCytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMREffects of genetic variants of human P450 oxidoreductase on catalysis by CYP2D6 in vitroCoupled motions direct electrons along human microsomal P450 ChainsNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Role of protein-protein interactions in cytochrome P450-mediated drug metabolism and toxicityDistinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.Transcriptional regulation of the human P450 oxidoreductase gene: hormonal regulation and influence of promoter polymorphisms.A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome cAltered human CYP3A4 activity caused by Antley-Bixler syndrome-related variants of NADPH-cytochrome P450 oxidoreductase measured in a robust in vitro systemConsequences of POR mutations and polymorphisms.Genetic variations in NADPH-CYP450 oxidoreductase in a Czech Slavic cohort.Phosphorylation of human cytochrome P450c17 by p38α selectively increases 17,20 lyase activity and androgen biosynthesis.Interactions between cytochromes P450 2B4 (CYP2B4) and 1A2 (CYP1A2) lead to alterations in toluene disposition and P450 uncouplingGating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase.Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes.Dynamic control of electron transfers in diflavin reductases.Towards the free energy landscape for catalysis in mammalian nitric oxide synthases.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Energy landscapes and catalysis in nitric-oxide synthase.Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.Molecular dynamics simulations give insight into the conformational change, complex formation, and electron transfer pathway for cytochrome P450 reductase.Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in Nanodiscs.The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specificElectron transfer by human wild-type and A287P mutant P450 oxidoreductase assessed by transient kinetics: functional basis of P450 oxidoreductase deficiency.Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome P450 reductase (POR) in nanodiscsConformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.Kinetics of electron transfer between NADPH-cytochrome P450 reductase and cytochrome P450 3A4.
P2860
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P2860
Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Domain motion in cytochrome P4 ...... small-angle x-ray scattering.
@en
type
label
Domain motion in cytochrome P4 ...... small-angle x-ray scattering.
@en
prefLabel
Domain motion in cytochrome P4 ...... small-angle x-ray scattering.
@en
P2093
P2860
P356
P1476
Domain motion in cytochrome P4 ...... d small-angle x-ray scattering
@en
P2093
Aldo Gutierrez
Igor L Barsukov
J Günter Grossmann
Jacqueline Ellis
P2860
P304
36628-36637
P356
10.1074/JBC.M109.054304
P407
P577
2009-10-26T00:00:00Z