A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina - Wikidata - wikimedia - TriplyDB

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

http://www.wikidata.org/entity/Q57003582

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A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II Geometric Restraint Drives On- and Off-pathway Catalysis by the Escherichia coli Menaquinol:Fumarate Reductase Mechanism of hydrogen activation by [NiFe] hydrogenases Structural and biochemical analyses reveal insights into covalent flavinylation of the Escherichia coli Complex II homolog quinol:fumarate reductase.Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the "oxaloacetate-inhibited" state.Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes.Catalytic mechanisms of complex II enzymes: a structural perspective Redox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR-1.The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS.Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase

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P2860

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

http://www.wikidata.org/entity/Q57003582

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im Mai 2006 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в травні 2006

@uk

name

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@en

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@nl

type

label

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@en

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@nl

prefLabel

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@en

A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina

@nl

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P1433

Journal of Biological Chemistry

P1476

A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina

@en

P2093

Anne K Jones

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Caroline S Miles

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

Christopher G Mowat

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Emma L Rothery

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Fraser A Armstrong

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Graeme A Reid

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Janette M Hudson

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Katherine L Pankhurst

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Stephen K Chapman

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P2860

Processing of X-ray diffraction data collected in oscillation mode

Open conformation of a flavocytochrome c3 fumarate reductase

Structural and mechanistic mapping of a unique fumarate reductase

Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1

Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution

Atomically defined mechanism for proton transfer to a buried redox centre in a protein

Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study

A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction

Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase

Engineering water to act as an active site acid catalyst in a soluble fumarate reductase

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20589-20597

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scholarly article

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10.1074/JBC.M603077200

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29

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281

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Malcolm Walkinshaw

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2006-05-12T00:00:00Z

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16699170

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