[NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states

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[NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1039/C4MT00309H
P698PubMed publication ID25780984
P5875ResearchGate publication ID273578326

P50authorAntonio L De LaceyQ51665904
Anne VolbedaQ54918209
Pierre-Pol LiebgottQ60015391
Juan C Fontecilla-CampsQ88328451
Lydie Martin-FaivreQ95607907
P2860cites workDirect Detection of a Hydrogen Ligand in the [NiFe] Center of the Regulatory H2-Sensing Hydrogenase fromRalstoniaeutrophain Its Reduced State by HYSCORE and ENDOR SpectroscopyQ44626341
A novel square-planar Ni(II) complex with an amino-carboxamido-dithiolato-type ligand as an active-site model of NiSOD.Q45413261
A single-crystal ENDOR and density functional theory study of the oxidized states of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.Q46808421
Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen--the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases.Q53341627
Nickel-dependent metalloenzymesQ24597659
Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolutionQ27618758
The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic centerQ27618761
Experimental approaches to kinetics of gas diffusion in hydrogenaseQ27651446
The Crystal Structure of the [NiFe] Hydrogenase from the Photosynthetic Bacterium Allochromatium vinosum: Characterization of the Oxidized Enzyme (Ni-A State)Q27663713
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centreQ27675093
Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenaseQ27675095
X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coliQ27678099
Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenaseQ27685146
Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenaseQ27690017
Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized statesQ27695711
Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenaseQ27697664
XDSQ27860472
Overview of the CCP4 suite and current developmentsQ27860782
REFMAC5 for the refinement of macromolecular crystal structuresQ27860905
Phasercrystallographic softwareQ27860930
Features and development of CootQ27861079
Nickel Superoxide Dismutase Structure and Mechanism†Q28314793
Structure/Function Relationships of [NiFe]- and [FeFe]-HydrogenasesQ29041302
AMoRe: an automated package for molecular replacementQ29642803
Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasisQ30859349
A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenaseQ34169576
Synthetic analogues of nickel superoxide dismutase: a new role for nickel in biology.Q34512797
Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicusQ34794910
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.Q35016350
Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutantsQ36471139
EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE.Q43583188
The structural plasticity of the proximal [4Fe3S] cluster is responsible for the O2 tolerance of membrane-bound [NiFe] hydrogenasesQ43854837
P433issue4
P407language of work or nameEnglishQ1860
P921main subjectnickelQ744
P304page(s)710-718
P577publication date2015-04-01
P1433published inMetallomicsQ3307262
P1476title[NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states
P478volume7

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cites work (P2860)
Q90122827Complete Protection of O2-Sensitive Catalysts in Thin Films
Q38501371Cyanobacterial hydrogenases and hydrogen metabolism revisited: recent progress and future prospects
Q26767154Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases
Q48105811Equilibrium between inactive ready Ni-SIr and active Ni-SIa states of [NiFe] hydrogenase studied by utilizing Ni-SIr-to-Ni-SIa photoactivation.
Q36085328Photoactivation of the Ni-SIr state to the Ni-SIa state in [NiFe] hydrogenase: FT-IR study on the light reactivity of the ready Ni-SIr state and as-isolated enzyme revisited

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