Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide.

Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide.

Rapid and reversible binding of sulfide to [NiFe]-hydrogenases (particularly the enzyme from Desulfovibrio vulgaris) under weakly acidic conditions (pH 6) has been studied by protein film voltammetry, which tracks the formation of different species as a function of potential. Sulfide (most likely en...

Bibliografske podrobnosti
Main Authors:	Vincent, K, Belsey, N, Lubitz, W, Armstrong, F
Format:	Journal article
Jezik:	English
Izdano:	2006

Podobne knjige/članki

Unusual reaction of [NiFe]-hydrogenases with cyanide.
od: Hexter, S, et al.
Izdano: (2014)

[NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates.
od: Armstrong, F, et al.
Izdano: (2005)

Hydrogen activation by [NiFe]-hydrogenases
od: Carr, S, et al.
Izdano: (2016)

Mechanism of hydrogen activation by [NiFe] hydrogenases
od: Evans, R, et al.
Izdano: (2015)

Mechanism of hydrogen activation by [NiFe] hydrogenases
od: Evans, R, et al.
Izdano: (2015)

Quantum chemical approaches to [NiFe] hydrogenase
od: Vaissier, Valerie, et al.
Izdano: (2018)

Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase.
od: Léger, C, et al.
Izdano: (2002)

The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide.
od: Lamle, SE, et al.
Izdano: (2005)

The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases
od: Pinske Constanze, et al.
Izdano: (2014-03-01)

A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases.
od: Cracknell, J, et al.
Izdano: (2009)

The importance of electron transfer in determining properties of [NiFe]-hydrogenases
od: Murphy, B
Izdano: (2013)

Importance of the active site "canopy" residues in an O2-tolerant [NiFe]-hydrogenase
od: Brooke, E, et al.
Izdano: (2016)

The Hydrogenase Subcomplex of the NAD(+)-Reducing [NiFe] Hydrogenase from Ralstonia eutropha - Insights into Catalysis and Redox Interconversions
od: Lauterbach, L, et al.
Izdano: (2011)

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

Infrared spectroelectrochemical study of E. coli NiFe hydrogenase 1
od: Gonzalez, R
Izdano: (2016)

Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.
od: Lukey, M, et al.
Izdano: (2011)

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.
od: Goris, T, et al.
Izdano: (2011)

Direct visible light activation of a surface cysteine-engineered [NiFe]-hydrogenase by silver nanoclusters
od: Zhang, L, et al.
Izdano: (2018)

Suppressing hydrogen peroxide generation to achieve oxygen-insensitivity of a [NiFe] hydrogenase in redox active films
od: Huaiguang Li, et al.
Izdano: (2020-02-01)

Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase.
od: Jones, A, et al.
Izdano: (2003)

Mechanistic exploitation of a self-repairing, blocked proton transfer pathway in an O2-tolerant [NiFe]-hydrogenase
od: Evans, R, et al.
Izdano: (2018)

Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.
od: Kwok-Ho Chan, et al.
Izdano: (2012-01-01)

The importance of the active site canopy in [NiFe]-hydrogenases from Escherichia coli
od: Beaton, S
Izdano: (2018)

Electrochemical and infrared spectroelectrochemical methods applied to the NiFe hydrogenases of Ralstonia eutropha
od: Liu, J
Izdano: (2012)

Dual role of HupF in the biosynthesis of [NiFe] hydrogenase <it>in Rhizobium leguminosarum</it>
od: Albareda Marta, et al.
Izdano: (2012-11-01)

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

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

Protein film infrared electrochemistry demonstrated for study of H2 oxidation by a [NiFe] hydrogenase
od: Ash, P, et al.
Izdano: (2017)

New insight into the mechanism of NiFe hydrogenases from IR spectroscopy coupled with protein film electrochemistry
od: Ash, P, et al.
Izdano: (2014)

Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha.
od: Lauterbach, L, et al.
Izdano: (2011)

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

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

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

Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha.
od: Lars Lauterbach, et al.
Izdano: (2011-01-01)

Oxygen-tolerant H2 oxidation by membrane-bound [NiFe] hydrogenases of ralstonia species. Coping with low level H2 in air.
od: Ludwig, M, et al.
Izdano: (2009)

Electrochemical and infrared spectroscopic studies provide insight into reactions of the NiFe regulatory hydrogenase from Ralstonia eutropha with O2 and CO
od: Ash, PA, et al.
Izdano: (2015)

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

[NiFe]-(Oxy)Sulfides Derived from NiFe<sub>2</sub>O<sub>4</sub> for the Alkaline Hydrogen Evolution Reaction
od: David Tetzlaff, et al.
Izdano: (2022-01-01)

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
od: Evans, RM, et al.
Izdano: (2024)

The electrochemical interconversions between the active and inactive states of a [NiFe]-hydrogenase; Implications for the development of a bio-fuel cell
od: Lamle, SE, et al.
Izdano: (2003)