Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism.
about
Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductaseCoupled motions direct electrons along human microsomal P450 ChainsCorrelating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic TrapNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer.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 cIn Vitro Biochemical Study of CYP51-Mediated Azole Resistance in Aspergillus fumigatusAzole Antifungal Sensitivity of Sterol 14α-Demethylase (CYP51) and CYP5218 from Malassezia globosaGating 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.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.Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes.Kinetic analysis of cytochrome P450 reductase from Artemisia annua reveals accelerated rates of NADH-dependent flavin reduction.Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase.Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface.Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate
P2860
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P2860
Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Inter-flavin electron transfer ...... idden complexity in mechanism.
@en
Inter-flavin electron transfer ...... idden complexity in mechanism.
@nl
type
label
Inter-flavin electron transfer ...... idden complexity in mechanism.
@en
Inter-flavin electron transfer ...... idden complexity in mechanism.
@nl
prefLabel
Inter-flavin electron transfer ...... idden complexity in mechanism.
@en
Inter-flavin electron transfer ...... idden complexity in mechanism.
@nl
P2860
P1433
P1476
Inter-flavin electron transfer ...... hidden complexity in mechanism
@en
P2093
Nigel S Scrutton
Sibylle Brenner
P2860
P304
P356
10.1111/J.1742-4658.2008.06597.X
P407
P577
2008-08-04T00:00:00Z