Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum - Test2 - elhamkhani - TriplyDB

Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Structure-function relationships in [FeFe]-hydrogenase active site maturation Genome, functional gene annotation, and nuclear transformation of the heterokont oleaginous alga Nannochloropsis oceanica CCMP1779 Philosophy of voltage-gated proton channels Expression of Shewanella oneidensis MR-1 [FeFe]-hydrogenase genes in Anabaena sp. strain PCC 7120 Insights into the structure and function of HV1 from a meta-analysis of mutation studies A threonine stabilizes the NiC and NiR catalytic intermediates of [NiFe]-hydrogenase.Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.Improvement of biocatalysts for industrial and environmental purposes by saturation mutagenesis Characterization of Hydrogen Metabolism in the Multicellular Green Alga Volvox carteri.A porous proton-relaying metal-organic framework material that accelerates electrochemical hydrogen evolution.Atypical effect of temperature tuning on the insertion of the catalytic iron-sulfur center in a recombinant [FeFe]-hydrogenase.The Physiological Functions and Structural Determinants of Catalytic Bias in the [FeFe]-Hydrogenases CpI and CpII of Clostridium pasteurianum Strain W5 Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.Protonation/reduction dynamics at the [4Fe-4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases.Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.Mechanism of O2 diffusion and reduction in FeFe hydrogenases.A reversible proton relay process mediated by hydrogen-bonding interactions in [FeFe]hydrogenase modeling.Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity.Heterologous Expression of the Clostridium carboxidivorans CO Dehydrogenase Alone or Together with the Acetyl Coenzyme A Synthase Enables both Reduction of CO2 and Oxidation of CO by Clostridium acetobutylicum.Spectroscopic investigations of a semi-synthetic [FeFe] hydrogenase with propane di-selenol as bridging ligand in the binuclear subsite: comparison to the wild type and propane di-thiol variants.Isotopic fractionation associated with [NiFe]- and [FeFe]-hydrogenases.A structural view of synthetic cofactor integration into [FeFe]-hydrogenases.Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

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P2860

Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

http://www.wikidata.org/entity/Q34214342

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2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

@en

Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

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JBC.M111.254664

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Journal of Biological Chemistry

P1476

Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum

@en

P2093

Adam J Cornish

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Eric L Hegg

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Hui Yang

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John W Peters

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Katrin Gärtner

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Dithiomethylether as a ligand in the hydrogenase h-cluster

Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)

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

Clustal W and Clustal X version 2.0

Structure-function relationships of anaerobic gas-processing metalloenzymes

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38341-38347

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10.1074/JBC.M111.254664

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44

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2011-09-07T00:00:00Z

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3207428

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