Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate

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Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome c

P2860

Q35755388-EA66D4BB-B11C-4810-A2F2-54EF4070FA86

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Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate

Item

http://www.wikidata.org/entity/Q57015763

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im August 2014 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published on 13 August 2014

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2014

@uk

name

Conformational change in cytochrome P450 reductase adsorbed at a Au

@nl

Conformational change in cytoc ...... adenine dinucleotide phosphate

@en

type

Item

label

Conformational change in cytochrome P450 reductase adsorbed at a Au

@nl

Conformational change in cytoc ...... adenine dinucleotide phosphate

@en

prefLabel

Conformational change in cytochrome P450 reductase adsorbed at a Au

@nl

Conformational change in cytoc ...... adenine dinucleotide phosphate

@en

P1476

Conformational change in cytoc ...... adenine dinucleotide phosphate

@en

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B Khara

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

J H Convery

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

P Harrison

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

P Weightman

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

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

Coupled motions direct electrons along human microsomal P450 Chains

The influence of the structure of the Au(110) surface on the ordering of a monolayer of cytochrome P450 reductase at the Au(110)/phosphate buffer interface.

Evidence for protein conformational change at a Au(110)/protein interface.

Determination of the structure of adenine monolayers adsorbed at Au(110)/electrolyte interfaces using reflection anisotropy spectroscopy.

Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism.

Electronic transition dipole moment directions of reduced anionic flavin in stretched poly(vinyl alcohol) films.

Electronic transitions in the isoalloxazine ring and orientation of flavins in model membranes studied by polarized light spectroscopy.

Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface.

Orientation of Ordered Structures of Cytosine and Cytidine5′-Monophosphate Adsorbed at Au(110)/Liquid Interfaces

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022708

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

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scholarly article

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10.1103/PHYSREVE.90.022708

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

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English

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

P478

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

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Nigel Scrutton

Caroline I. Smith

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2014-08-13T00:00:00Z

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

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25215759

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Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate

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P2860

P2860

Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698