A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase.
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Experimental approaches to kinetics of gas diffusion in hydrogenaseStructural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenaseCrystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized statesHydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenaseMechanism of hydrogen activation by [NiFe] hydrogenasesDensity functional study of the catalytic cycle of nickel-iron [NiFe] hydrogenases and the involvement of high-spin nickel(II)A threonine stabilizes the NiC and NiR catalytic intermediates of [NiFe]-hydrogenase.Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianumAnalyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases.Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy.The Physiological Functions and Structural Determinants of Catalytic Bias in the [FeFe]-Hydrogenases CpI and CpII of Clostridium pasteurianum Strain W5Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C IntermediateRetuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Pathways of H2 toward the active site of [NiFe]-hydrogenase.The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis.Theoretical insights into [NiFe]-hydrogenases oxidation resulting in a slowly reactivating inactive state.Theoretical investigation of aerobic and anaerobic oxidative inactivation of the [NiFe]-hydrogenase active site.The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping.How are the ready and unready states of nickel-iron hydrogenase activated by H2? A density functional theory study.A Proton Delivery Pathway in the Soluble Fumarate Reductase fromShewanella frigidimarina
P2860
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P2860
A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase.
description
2003 nî lūn-bûn
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2003年の論文
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name
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@en
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@nl
type
label
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@en
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@nl
prefLabel
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@en
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@nl
P2093
P2860
P356
P1476
A glutamate is the essential p ...... cle of the [NiFe] hydrogenase.
@en
P2093
Alejandro Pardo
Antonio L De Lacey
Bruno Guigliarelli
Bénédicte Burlat
Géraldine Adryanczyk-Perrier
Marc Rousset
Sébastien Dementin
Victor M Fernandez
P2860
P304
10508-10513
P356
10.1074/JBC.M312716200
P407
P577
2003-12-20T00:00:00Z