(Q27675095)

1

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Ki-Seok Yoon

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Hirofumi Nishihara

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Yoshiki Higuchi

Occurrence, classification, and biological function of hydrogenases: an overview.

4

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language of work or name

English

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publication date

16 October 2011

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published in

Nature

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volume

479

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issue

7372

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page(s)

253-6

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cites work

1 reference

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Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels

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How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

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Activation and inactivation of hydrogenase function and the catalytic cycle: spectroelectrochemical studies.

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[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation

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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

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Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis

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Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics.

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[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3

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

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Spectroscopic insights into the oxygen-tolerant membrane-associated [NiFe] hydrogenase of Ralstonia eutropha H16

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Redox-dependent structural changes in the nitrogenase P-cluster

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Structural Basis for the Mechanism of Respiratory Complex I

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Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 A resolution

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Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold

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

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

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A glutamate is the essential proton transfer gate during the catalytic cycle of the [NiFe] hydrogenase

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[NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques

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

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The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state

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Enlarging the gas access channel to the active site renders the regulatory hydrogenase HupUV of Rhodobacter capsulatus O2 sensitive without affecting its transductory activity.

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Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus

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Processing of X-ray diffraction data collected in oscillation mode

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The CCP4 suite: programs for protein crystallography

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Refinement of macromolecular structures by the maximum-likelihood method

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A short history of SHELX

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Coot: model-building tools for molecular graphics

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Proton pathways in a [NiFe]-hydrogenase: A theoretical study

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PubMed

https://pubmed.ncbi.nlm.nih.gov/22002607

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

[NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus: properties, function, and phylogenetics.

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22002607

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Immobilization of the hyperthermophilic hydrogenase from Aquifex aeolicus bacterium onto gold and carbon nanotube electrodes for efficient H2 oxidation

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22002607