Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding - Wikidata - wikimedia - TriplyDB

Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding

Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding

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The syndrome of 17,20 lyase deficiency Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency Structural diversity of eukaryotic membrane cytochrome p450s ubiI,a New Gene inEscherichia coliCoenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation Coupled motions direct electrons along human microsomal P450 Chains Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Role of protein-protein interactions in cytochrome P450-mediated drug metabolism and toxicity Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Heme enzyme structure and function.Distinct 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.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 c The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Bio-inspired electron-delivering system for reductive activation of dioxygen at metal centres towards artificial flavoenzymes.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Interactions between CYP2E1 and CYP2B4: effects on affinity for NADPH-cytochrome P450 reductase and substrate metabolism.Human cytochromes P450 in health and disease Redox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone Interactions between cytochromes P450 2B4 (CYP2B4) and 1A2 (CYP1A2) lead to alterations in toluene disposition and P450 uncoupling Correlation of Cytochrome P450 Oxidoreductase Expression with the Expression of 10 Isoforms of Cytochrome P450 in Human Liver.Gating 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.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.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.The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.Electron transfer by human wild-type and A287P mutant P450 oxidoreductase assessed by transient kinetics: functional basis of P450 oxidoreductase deficiency.RNA interference of NADPH-cytochrome P450 reductase of the rice brown planthopper, Nilaparvata lugens, increases susceptibility to insecticides.Kinetic analysis of cytochrome P450 reductase from Artemisia annua reveals accelerated rates of NADH-dependent flavin reduction.The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.Application of methyl-TROSY to a large paramagnetic membrane protein without perdeuteration: 13C-MMTS-labeled NADPH-cytochrome P450 oxidoreductase.Structural and Kinetic Studies of Asp632 Mutants and Fully Reduced NADPH-Cytochrome P450 Oxidoreductase Define the Role of Asp632 Loop Dynamics in the Control of NADPH Binding and Hydride Transfer.Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase.Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strength

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Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding

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2011 nî lūn-bûn

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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2011年の論文

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Conformational Changes of NADP ...... Catalysis and Cofactor Binding

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Charles B Kasper

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A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

Hydrocarbon hydroxylation by cytochrome P450 enzymes

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes

Processing of X-ray diffraction data collected in oscillation mode

NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer

Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

Coot: model-building tools for molecular graphics

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