about
More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicusAnalytical approaches to photobiological hydrogen production in unicellular green algaeNADPH-generating systems in bacteria and archaeaThe modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implicationsX-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritimaThe crystal structure of [Fe]-hydrogenase reveals the geometry of the active siteThe crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complexStepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)Structural Basis for the Reaction Mechanism of S-Carbamoylation of HypE by HypF in the Maturation of [NiFe]-HydrogenasesProtein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactorTowards a functional identification of catalytically inactive [Fe]-hydrogenase paralogsMicrobial-based motor fuels: science and technologyReversible oxygen-tolerant hydrogenase carried by free-living N2-fixing bacteria isolated from the rhizospheres of rice, maize, and wheatCharacterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS).In silico evaluation of proposed biosynthetic pathways for the unique dithiolate ligand of the H-cluster of [FeFe]-hydrogenase.Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosumGenomic characterization of methanomicrobiales reveals three classes of methanogens.Comprehensive computational analysis of Hmd enzymes and paralogs in methanogenic ArchaeaIdentification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor.A model for the CO-inhibited form of [NiFe] hydrogenase: synthesis of CO3Fe(micro-StBu)3Ni{SC6H3-2,6-(mesityl)2} and reversible CO addition at the Ni site.Towards artificial leaves for solar hydrogen and fuels from carbon dioxide.The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy study.Fe-H/D stretching and bending modes in nuclear resonant vibrational, Raman and infrared spectroscopies: comparisons of density functional theory and experiment.Regioselectivity of H cluster oxidation.Iron acyl thiolato carbonyls: structural models for the active site of the [Fe]-hydrogenase (Hmd).In-silico identification of phenotype-biased functional modules.Thiolate-bridged dinuclear iron(tris-carbonyl)-nickel complexes relevant to the active site of [NiFe] hydrogenase.Radical S-adenosylmethionine enzymes.[Fe]-hydrogenase and models that contain iron-acyl ligation.De novo design of functional proteins: Toward artificial hydrogenases.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Models for the hydrogenases put the focus where it should be--hydrogen.Importance of the protein framework for catalytic activity of [FeFe]-hydrogenases.Identification of a novel class of membrane-bound [NiFe]-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis.Linking energy production and protein synthesis in hydrogenotrophic methanogensNADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO.The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases.Mutational Analyses of the Enzymes Involved in the Metabolism of Hydrogen by the Hyperthermophilic Archaeon Pyrococcus furiosus.Nature's hydrides: rapid reduction of halocarbons by folate model compoundsAn iron(II) carbonyl thiolato complex bearing 2-methoxy-pyridine: a structural model of the active site of [Fe] hydrogenase.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
name
A third type of hydrogenase catalyzing H2 activation.
@ast
A third type of hydrogenase catalyzing H2 activation.
@en
A third type of hydrogenase catalyzing H2 activation.
@nl
type
label
A third type of hydrogenase catalyzing H2 activation.
@ast
A third type of hydrogenase catalyzing H2 activation.
@en
A third type of hydrogenase catalyzing H2 activation.
@nl
prefLabel
A third type of hydrogenase catalyzing H2 activation.
@ast
A third type of hydrogenase catalyzing H2 activation.
@en
A third type of hydrogenase catalyzing H2 activation.
@nl
P2860
P356
P1433
P1476
A third type of hydrogenase catalyzing H2 activation.
@en
P2093
Rudolf K Thauer
Seigo Shima
P2860
P356
10.1002/TCR.20111
P577
2007-01-01T00:00:00Z