The active site and catalytic mechanism of NiFe hydrogenases - Wikidata - awgldk - TriplyDB

The active site and catalytic mechanism of NiFe hydrogenases

The active site and catalytic mechanism of NiFe hydrogenases

http://www.wikidata.org/entity/Q57483432

about

NAD(H)-coupled hydrogen cycling - structure-function relationships of bidirectional [NiFe] hydrogenases Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein Metabolically engineered bacteria for producing hydrogen via fermentation Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Modelling NiFe hydrogenases: nickel-based electrocatalysts for hydrogen production.The roles of the first and second coordination spheres in the design of molecular catalysts for H2 production and oxidation.Proton reduction to hydrogen in biological and chemical systems.Towards [NiFe]-hydrogenase biomimetic models that couple H2 binding with functionally relevant intramolecular electron transfers: a quantum chemical study.Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation.Structural and gene expression analyses of uptake hydrogenases and other proteins involved in nitrogenase protection in Frankia.A Ni(i)Fe(ii) analogue of the Ni-L state of the active site of the [NiFe] hydrogenases.Exploration of H2 binding to the [NiFe]-hydrogenase active site with multiconfigurational density functional theory.Amino olefin nickel(i) and nickel(0) complexes as dehydrogenation catalysts for amine boranes

P2860

Q27011364-ACF142DB-AB9A-41FC-BA92-87131A2B163D Q27646545-13FE2AFA-A0D5-409D-B548-CAA17834BBAB Q28661095-E25BB678-8C55-4BD4-A2EE-4167E0E2F584 Q35796174-62DB61B5-6F75-4644-A231-A6D739DA4E42 Q37138317-9A2C0BD9-7C4D-4B1A-BE1B-7C8AF06AFD78 Q37352679-A35ADE86-3929-4F23-9413-7C7E5D35C937 Q38042317-B3DFC828-2559-4C96-A06D-E59E1E64F2AE Q39371280-CA268C1D-E9C7-4B0E-8029-D96AF2665EFD Q42699139-2ADDBDAB-8583-48B8-AA87-2FCB44CD331C Q43622644-5FCCF804-F246-4314-AE89-4A4626877FA0 Q46657908-EF3925B6-6F48-46E4-8C19-01F24630790F Q48181297-5CE3B45D-745A-4944-AE79-AAEDD129E033 Q56743436-669F69DF-7741-4249-84D4-21D577EC450D

P2860

The active site and catalytic mechanism of NiFe hydrogenases

http://www.wikidata.org/entity/Q57483432

description

im Januar 2003 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована у 2003

@uk

name

The active site and catalytic mechanism of NiFe hydrogenases

@en

The active site and catalytic mechanism of NiFe hydrogenases

@nl

type

label

The active site and catalytic mechanism of NiFe hydrogenases

@en

The active site and catalytic mechanism of NiFe hydrogenases

@nl

prefLabel

The active site and catalytic mechanism of NiFe hydrogenases

@en

The active site and catalytic mechanism of NiFe hydrogenases

@nl

P1433

Q57483432-BFCA093F-C064-4F4B-A8E2-7616E53EFC00

P1476

Q57483432-615E8EA5-528C-49B2-8C7D-ACAB1D90DC57

P2093

Q57483432-0013DE92-E0F5-4CC6-BBEA-C2719F0F4917

Q57483432-74B8261E-FDF6-4A49-8449-A05F018A07C5

P2860

Q57483432-01268142-46BC-4151-AE0F-1BFC4DB8F45A

Q57483432-08661A0F-C67D-48A9-8CCB-9ABD2FB98ECA

Q57483432-102AEB88-1668-41C4-BA71-BB6F2C086E12

Q57483432-11220849-2444-4769-811A-9A9763AB35CB

Q57483432-14BB70A1-DA1C-4693-96E0-194A6CF586DC

Q57483432-17D0A286-E44E-45EA-8A8E-853FD25175DF

Q57483432-3462F292-346F-4648-BE6A-239938693581

Q57483432-379A03BF-EF78-4E38-A229-A9CC58BA3C79

Q57483432-482680B2-D1BD-4197-9C13-5B111BA8F673

Q57483432-4BE5C29D-B379-4BD5-B05A-C1315B404835

P304

Q57483432-62BF7005-B4E3-41CA-8879-E4DACA200AF6

P31

Q57483432-EF2BCCCA-303E-4522-913B-C8FCFDACD872

P356

Q57483432-A3B83FFD-A11E-48E5-8396-8B4966F75E73

P407

Q57483432-3F45A8A1-C6EE-405A-B154-0A8C9539E036

P433

Q57483432-396554F9-ACBC-46D3-98C7-4D276F5717E7

P577

Q57483432-4E1A47A7-1107-49EE-B0FB-10F25BCBF6F0

P356

P1433

Dalton Transactions

P1476

The active site and catalytic mechanism of NiFe hydrogenases

@en

P2093

Anne Volbeda

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

Juan C. Fontecilla-Camps

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

P2860

Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus

Hydrogen production. Green algae as a source of energy

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

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

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

[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

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

Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

P304

4030-4038

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

P31

scholarly article

P356

10.1039/B304316A

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

P407

P433

21

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

P577

2003-01-01T00:00:00Z

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