Hydrogen activation by [NiFe]-hydrogenases

Hydrogen activation by [NiFe]-hydrogenases

Hydrogenase-1 (Hyd-1) from Escherichia coli is a membrane-bound enzyme that catalyses the reversible oxidation of molecular H2 The active site contains one Fe and one Ni atom and several conserved amino acids including an arginine (Arg(509)), which interacts with two conserved aspartate residues (As...

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Bibliografische gegevens
Hoofdauteurs:	Carr, S, Evans, R, Brooke, E, Wehlin, S, Nomerotskaia, E, Sargent, F, Armstrong, F, Phillips, S
Formaat:	Journal article
Taal:	English
Gepubliceerd in:	Portland Press 2016

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Importance of the active site "canopy" residues in an O2-tolerant [NiFe]-hydrogenase
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The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide.
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Unusual reaction of [NiFe]-hydrogenases with cyanide.
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Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase.
door: Léger, C, et al.
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Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide.
door: Vincent, K, et al.
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[NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates.
door: Armstrong, F, et al.
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Mechanistic exploitation of a self-repairing, blocked proton transfer pathway in an O2-tolerant [NiFe]-hydrogenase
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Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.
door: Lukey, M, et al.
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Direct visible light activation of a surface cysteine-engineered [NiFe]-hydrogenase by silver nanoclusters
door: Zhang, L, et al.
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Quantum chemical approaches to [NiFe] hydrogenase
door: Vaissier, Valerie, et al.
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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.
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The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases
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A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases.
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Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production
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Exploration of proton transfer pathways in the oxygen-tolerant [NiFe]-hydrogenase from Escherichia coli
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The importance of electron transfer in determining properties of [NiFe]-hydrogenases
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Zymographic differentiation of [NiFe]-Hydrogenases 1, 2 and 3 of <it>Escherichia coli</it> K-12
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Infrared spectroelectrochemical study of E. coli NiFe hydrogenase 1
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Principles of hydrogen catalysis in the presence of oxygen by a [NiFe] hydrogenase from E. coli
door: Wulff, P
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The importance of the active site canopy in [NiFe]-hydrogenases from Escherichia coli
door: Beaton, S
Gepubliceerd in: (2018)

Suppressing hydrogen peroxide generation to achieve oxygen-insensitivity of a [NiFe] hydrogenase in redox active films
door: Huaiguang Li, et al.
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A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.
door: Goris, T, et al.
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Minimal Influence of [NiFe] Hydrogenase on Hydrogen Isotope Fractionation in H2-Oxidizing Cupriavidus necator
door: Brian J. Campbell, et al.
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Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase.
door: Jones, A, et al.
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The electrochemical interconversions between the active and inactive states of a [NiFe]-hydrogenase; Implications for the development of a bio-fuel cell
door: Lamle, SE, et al.
Gepubliceerd in: (2003)

The Hydrogenase Subcomplex of the NAD(+)-Reducing [NiFe] Hydrogenase from Ralstonia eutropha - Insights into Catalysis and Redox Interconversions
door: Lauterbach, L, et al.
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Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.
door: Kwok-Ho Chan, et al.
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Electrochemical and infrared spectroelectrochemical methods applied to the NiFe hydrogenases of Ralstonia eutropha
door: Liu, J
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Dual role of HupF in the biosynthesis of [NiFe] hydrogenase <it>in Rhizobium leguminosarum</it>
door: Albareda Marta, et al.
Gepubliceerd in: (2012-11-01)

Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in <it>Escherichia coli</it>
door: Kim Jaoon YH, et al.
Gepubliceerd in: (2010-07-01)

Synthesis, Structures and Chemical Reactivity of Dithiolato-Bridged Ni-Fe Complexes as Biomimetics for the Active Site of [NiFe]-Hydrogenases
door: Li-Cheng Song, et al.
Gepubliceerd in: (2022-06-01)

Proton transfer in the catalytic cycle of NiFe hydrogenases: insight from vibrational spectroscopy
door: Ash, P, et al.
Gepubliceerd in: (2017)

Unifying activity, structure, and spectroscopy of [NiFe] hydrogenases: Combining techniques to clarify mechanistic understanding
door: Ash, PA, et al.
Gepubliceerd in: (2019)

Replacing a cysteine ligand by selenocysteine in a [NiFe]-hydrogenase unlocks hydrogen production activity and addresses the role of concerted proton-coupled electron transfer in electrocatalytic reversibility
door: Evans, RM, et al.
Gepubliceerd in: (2024)

Mechanistic studies of H2 oxidation and evolution catalysed by NiFe hydrogenase enzymes
door: Kendall-Price, S
Gepubliceerd in: (2022)

Heterologous expression of Alteromonas macleodii and Thiocapsa roseopersicina [NiFe] hydrogenases in Synechococcus elongatus.
door: Philip D Weyman, et al.
Gepubliceerd in: (2011-01-01)

[NiFe]-hydrogenases are constitutively expressed in an enriched Methanobacterium sp. population during electromethanogenesis.
door: Elisabet Perona-Vico, et al.
Gepubliceerd in: (2019-01-01)

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.
door: Roessler, M, et al.
Gepubliceerd in: (2012)