X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli - Wikidata - wikimedia - TriplyDB

X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli

X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli

http://www.wikidata.org/entity/Q27678099

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Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases De novo modeling of the F 420 -reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenase Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized states [NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states Mechanism of hydrogen activation by [NiFe] hydrogenases Krypton Derivatization of an O2 -Tolerant Membrane-Bound [NiFe] Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas Transport Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl-Group Channeling during [NiFe]-Hydrogenase Cofactor Generation A threonine stabilizes the NiC and NiR catalytic intermediates of [NiFe]-hydrogenase.Genome annotation provides insight into carbon monoxide and hydrogen metabolism in Rubrivivax gelatinosus.How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases.Zymographic differentiation of [NiFe]-hydrogenases 1, 2 and 3 of Escherichia coli K-12.Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum Metagenomic Sequencing Unravels Gene Fragments with Phylogenetic Signatures of O2-Tolerant NiFe Membrane-Bound Hydrogenases in Lacustrine Sediment Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants.Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mossbauer and EPR spectroscopy.The Mössbauer Parameters of the Proximal Cluster of Membrane-Bound Hydrogenase Revisited: A Density Functional Theory Study Structure, function and biosynthesis of O₂-tolerant hydrogenases.Rubredoxin-related maturation factor guarantees metal cofactor integrity during aerobic biosynthesis of membrane-bound [NiFe] hydrogenase How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure.Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy.Structure and function of [NiFe] hydrogenases.Carbon nanofiber mesoporous films: efficient platforms for bio-hydrogen oxidation in biofuel cells.Complexes of Ni(i): a "rare" oxidation state of growing importance.Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli.Electronic states of the O2-tolerant [NiFe] hydrogenase proximal cluster.Reply to Mouesca et al.: Electronic structure of the proximal [4Fe-3S] cluster of O2-tolerant [NiFe] hydrogenases.The structural plasticity of the proximal [4Fe3S] cluster is responsible for the O2 tolerance of membrane-bound [NiFe] hydrogenases.Microbial hydrogen splitting in the presence of oxygen.Light-induced reactivation of O2-tolerant membrane-bound [Ni-Fe] hydrogenase from the hyperthermophilic bacterium Aquifex aeolicus under turnover conditions.A regulatory domain controls the transport activity of a twin-arginine signal peptide.Reactivation from the Ni-B state in [NiFe] hydrogenase of Ralstonia eutropha is controlled by reduction of the superoxidised proximal cluster.Signal peptide etiquette during assembly of a complex respiratory enzyme.

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X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli

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2012 nî lūn-bûn

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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年论文

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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Proceedings of the National Academy of Sciences of the United States of America

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X-ray crystallographic and com ...... genase 1 from Escherichia coli

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P2093

Claudine Darnault

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Fraser A Armstrong

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Jean-Marie Mouesca

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Juan C Fontecilla-Camps

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Patricia Amara

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P2860

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

The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A state)

The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre

Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase

Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata

Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus.

A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases.

A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin.

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5305-10

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4908654

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10.1073/PNAS.1119806109

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Maxie M Roessler

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2012-04-03T00:00:00Z

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