Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.

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Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.Nanodiscs in Membrane Biochemistry and Biophysics.Spectroscopic studies of the cytochrome P450 reaction mechanisms.

P2860

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P2860

Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.

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http://www.wikidata.org/entity/Q40124142

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

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2016年論文

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2016年論文

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2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

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name

Role of the Proximal Cysteine ...... Double Resonance Spectroscopy.

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type

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Role of the Proximal Cysteine ...... Double Resonance Spectroscopy.

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Role of the Proximal Cysteine ...... Double Resonance Spectroscopy.

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P1476

Role of the Proximal Cysteine ...... Double Resonance Spectroscopy.

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P2093

Brian M Hoffman

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Lucy Waskell

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Muralidharan Shanmugam

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Naw May Pearl

http://www.w3.org/2001/XMLSchema#string

Roman Davydov

http://www.w3.org/2001/XMLSchema#string

Sangchoul Im

http://www.w3.org/2001/XMLSchema#string

William A Gunderson

http://www.w3.org/2001/XMLSchema#string

P2860

Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase

The catalytic pathway of cytochrome p450cam at atomic resolution

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3

Oxygen activation and electron transfer in flavocytochrome P450 BM3

Structural and Functional Characterization of a Cytochrome P450 2B4 F429H Mutant with an Axial Thiolate–Histidine Hydrogen Bond

Laser flash photolysis generation of high-valent transition metal-oxo species: insights from kinetic studies in real time.

Kinetics of oxidation of benzphetamine by compounds I of cytochrome P450 2B4 and its mutants.

EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from Geobacillus stearothermophilus.

Electron paramagnetic resonance study of the high- and low-spin forms of cytochrome P-450 in liver and in liver microsomes from a methylcholanthrene-treated rabbit

Sulfur K-edge XAS and DFT calculations on P450 model complexes: effects of hydrogen bonding on electronic structure and redox potentials

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869-883

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scholarly article

P356

10.1021/ACS.BIOCHEM.5B00744

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English

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2016-01-10T00:00:00Z

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26750753

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4834902

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Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.

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P2860

P2860

Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932