Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
about
Structural 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 NMRKinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.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.Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome cSingle-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics studyTowards 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.A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.A perspective on conformational control of electron transfer in nitric oxide synthases.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.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.Solution structure of the cytochrome P450 reductase-cytochrome c complex determined by neutron scattering.Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strengthA promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion.Lipid-exchange in nanodiscs discloses membrane boundaries of cytochrome-P450 reductase
P2860
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P2860
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
@en
type
label
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
@en
prefLabel
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
@en
P2860
P50
P1433
P1476
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
@en
P2093
Gordon C K Roberts
Jacqueline Ellis
P2860
P304
P356
10.1016/J.STR.2013.06.022
P577
2013-08-01T00:00:00Z