A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase (Q44701420)

5 December 2017

title

A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase (English)

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5 December 2017

Sébastien Dementin

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5 December 2017

Bénédicte Burlat

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5 December 2017

Antonio L De Lacey

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5 December 2017

Alejandro Pardo

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5 December 2017

Géraldine Adryanczyk-Perrier

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5 December 2017

Bruno Guigliarelli

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5 December 2017

Victor M Fernandez

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5 December 2017

Marc Rousset

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5 December 2017

language of work or name

English

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publication date

20 December 2003

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Journal of Biological Chemistry

5 December 2017

published in

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5 December 2017

volume

279

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5 December 2017

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5 December 2017

page(s)

10508-10513

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X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution

5 December 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Natural engineering principles of electron tunnelling in biological oxidation-reduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

[3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Bioenergetics. Purpose of proton pathways.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

New shuttle vectors for the introduction of cloned DNA in Desulfovibrio

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Marker exchange mutagenesis of the hydN genes in Desulfovibrio fructosovorans.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Nickel hydrogenases: in search of the active site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

The low barrier hydrogen bond in enzymatic catalysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Functional analysis by site-directed mutagenesis of the NAD(+)-reducing hydrogenase from Ralstonia eutropha.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Biological activition of hydrogen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Kinetic studies on hydrogenase. Parahydrogen-orthohydrogen conversion and hydrogen-deuterium exchange reactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Liberation of hydrogen sulfide during the catalytic action of Desulfovibrio hydrogenase under the atmosphere of hydrogen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

The bio-organometallic chemistry of active site iron in hydrogenases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

17O ENDOR Detection of a Solvent-Derived Ni−(OHx)−Fe Bridge That Is Lost upon Activation of the Hydrogenase fromDesulfovibrio gigas

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Is there a rate-limiting step in the catalytic cycle of Ni-Fe hydrogenases?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

The [NiFe] hydrogenase from Allochromatium vinosum studied in EPR-detectable states: H/D exchange experiments that yield new information about the structure of the active site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Nature and electronic structure of the Ni-X dinuclear center of Desulfovibrio gigas hydrogenase. Implications for the enzymatic mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovoransNi-Fe hydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Kinetic characterization of Desulfovibrio gigas hydrogenase upon selective chemical modification of amino acid groups as a tool for structure-function relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Structural organization of the Ni and (4Fe-4S) centers in the active form of Desulfovibrio gigas hydrogenase. Analysis of the magnetic interactions by electron paramagnetic resonance spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

Spin-spin interactions between the Ni site and the [4Fe-4S] centers as a probe of light-induced structural changes in active Desulfovibrio gigas hydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312716200

21 January 2018

Identifiers

DOI

10.1074/JBC.M312716200

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5 December 2017

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