The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site - Wikidata - wikimedia - TriplyDB

The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella paludicola, the first cultivated representative of the order Methanocellales Analytical approaches to photobiological hydrogen production in unicellular green algae Multidisciplinary approaches to solar hydrogen Structure-function relationships in [FeFe]-hydrogenase active site maturation NAD(H)-coupled hydrogen cycling - structure-function relationships of bidirectional [NiFe] hydrogenases The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex Crystal structures of [Fe]-hydrogenase in complex with inhibitory isocyanides: implications for the H2-activation site Identification of the HcgB enzyme in [Fe]-hydrogenase-cofactor biosynthesis A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor Towards a functional identification of catalytically inactive [Fe]-hydrogenase paralogs Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis A simple complex on the verge of breakdown: isolation of the elusive cyanoformate ion Tyrosine, cysteine, and S-adenosyl methionine stimulate in vitro [FeFe] hydrogenase activation Nitrogen fixation and hydrogen metabolism in cyanobacteria Nitric oxide activation by distal redox modulation in tetranuclear iron nitrosyl complexes Biomimetic chemistry of iron, nickel, molybdenum, and tungsten in sulfur-ligated protein sites.In silico evaluation of proposed biosynthetic pathways for the unique dithiolate ligand of the H-cluster of [FeFe]-hydrogenase.Small molecule mimics of hydrogenases: hydrides and redox.Quantitative proteomics of nutrient limitation in the hydrogenotrophic methanogen Methanococcus maripaludis.Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor.The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy study.Adenosyl radical: reagent and catalyst in enzyme reactions.Fe-H/D stretching and bending modes in nuclear resonant vibrational, Raman and infrared spectroscopies: comparisons of density functional theory and experiment.Trace metal requirements for microbial enzymes involved in the production and consumption of methane and nitrous oxide.Iron acyl thiolato carbonyls: structural models for the active site of the [Fe]-hydrogenase (Hmd).Connecting [NiFe]- and [FeFe]-hydrogenases: mixed-valence nickel-iron dithiolates with rotated structures Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival Amidine dications: isolation and [Fe]-hydrogenase-related hydrogenation Amidine dications as superelectrophiles Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.H2 metabolism is widespread and diverse among human colonic microbes Radical S-adenosylmethionine enzymes.Evolution in the understanding of [Fe]-hydrogenase.Beyond structural genomics: computational approaches for the identification of ligand binding sites in protein structures.Studies on hydrogenase.[Fe]-hydrogenase and models that contain iron-acyl ligation.The use and misuse of photosynthesis in the quest for novel methods to harness solar energy to make fuel.Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.The broadening reach of frustrated Lewis pair chemistry.

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

http://www.wikidata.org/entity/Q27651339

description

2008 nî lūn-bûn

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2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2008 թվականի հուլիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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type

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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SCIENCE.1158978

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

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Marco S Stagni

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

Michael Schick

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

Oliver Pilak

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Rudolf K Thauer

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Seigo Shima

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

Sonja Vogt

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

Wolfram Meyer-Klaucke

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

P2860

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

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

Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum

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

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

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

The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif

The coordination chemistry of 2-pyridone and its derivatives

A dinuclear Ni(mu-H)Ru complex derived from H2.

Hydrogenases: hydrogen-activating enzymes.

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572-5

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scholarly article

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3329366

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10.1126/SCIENCE.1158978

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5888

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321

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Eberhard Warkentin

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2008-07-25T00:00:00Z

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51427302

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18653896

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crystal structure