Characterization of the microsomal cytochrome P450 2B4 O2 activation intermediates by cryoreduction and electron paramagnetic resonance.
about
Structural and Functional Characterization of a Cytochrome P450 2B4 F429H Mutant with an Axial Thiolate–Histidine Hydrogen BondF429 Regulation of Tunnels in Cytochrome P450 2B4: A Top Down Study of Multiple Molecular Dynamics SimulationsCytochromes P450 in nanodiscs.Reactive intermediates in cytochrome p450 catalysis.Compound I is the reactive intermediate in the first monooxygenation step during conversion of cholesterol to pregnenolone by cytochrome P450scc: EPR/ENDOR/cryoreduction/annealing studies.Experimental documentation of the structural consequences of hydrogen-bonding interactions to the proximal cysteine of a cytochrome P450.Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing StudiesComparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction StudiesSpectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.The use of deuterated camphor as a substrate in (1)H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound IThe critical iron-oxygen intermediate in human aromataseActive intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.Spectroscopic features of cytochrome P450 reaction intermediatesHuman aromatase: perspectives in biochemistry and biotechnology.Nanodiscs in Membrane Biochemistry and Biophysics.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.Stabilization and spectroscopic characterization of the dioxygen complex of wild-type cytochrome P4502B4 (CYP2B4) and its distal side E301Q, T302A and proximal side F429H mutants at subzero temperatures.Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates.A single-site mutation (F429H) converts the enzyme CYP 2B4 into a heme oxygenase: a QM/MM study.Arene activation by a nonheme iron(III)-hydroperoxo complex: pathways leading to phenol and ketone products.
P2860
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P2860
Characterization of the microsomal cytochrome P450 2B4 O2 activation intermediates by cryoreduction and electron paramagnetic resonance.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
@zh-hans
2008年学术文章
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2008年学术文章
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2008年學術文章
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2008年學術文章
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name
Characterization of the micros ...... ectron paramagnetic resonance.
@en
Characterization of the micros ...... ectron paramagnetic resonance.
@nl
type
label
Characterization of the micros ...... ectron paramagnetic resonance.
@en
Characterization of the micros ...... ectron paramagnetic resonance.
@nl
prefLabel
Characterization of the micros ...... ectron paramagnetic resonance.
@en
Characterization of the micros ...... ectron paramagnetic resonance.
@nl
P2093
P2860
P356
P1433
P1476
Characterization of the micros ...... ectron paramagnetic resonance.
@en
P2093
Brian M Hoffman
Lucy Waskell
Reza Razeghifard
Roman Davydov
Sang-Choul Im
P2860
P304
P356
10.1021/BI800926X
P407
P577
2008-08-13T00:00:00Z