Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.

Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.

An important clue to the mechanism for O(2) tolerance of certain [NiFe]-hydrogenases is the conserved presence of a modified environment around the iron-sulfur cluster that is proximal to the active site. The O(2)-tolerant enzymes contain two cysteines, located at opposite ends of this cluster, whic...

Full description

Bibliographic Details
Main Authors:	Lukey, M, Roessler, M, Parkin, A, Evans, R, Davies, R, Lenz, O, Friedrich, B, Sargent, F, Armstrong, F
Format:	Journal article
Language:	English
Published:	2011

Similar Items

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

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

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

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.
by: Evans, R, et al.
Published: (2013)

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

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

Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide.
by: Vincent, K, et al.
Published: (2006)

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

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

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.
by: Roessler, M, et al.
Published: (2012)

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

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

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

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

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

X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli.
by: Volbeda, A, et al.
Published: (2012)

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

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

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

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

Zymographic differentiation of [NiFe]-Hydrogenases 1, 2 and 3 of <it>Escherichia coli</it> K-12
by: Pinske Constanze, et al.
Published: (2012-07-01)

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

Discovery of dark pH-dependent H+ migration in a [NiFe]-hydrogenase and its mechanistic relevance: mobilizing the hydrido ligand of the Ni-C intermediate
by: Murphy, BJ, et al.
Published: (2015)

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

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

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

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

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

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

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

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

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

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

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

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

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

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
by: Evans, RM, et al.
Published: (2024)

Retuning the catalytic bias and overpotential of a [NiFe]-hydrogenase via a single amino acid exchange at the electron entry/exit site
by: Adamson, H, et al.
Published: (2017)

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

Genome-Scale Mining of Acetogens of the Genus Clostridium Unveils Distinctive Traits in [FeFe]- and [NiFe]-Hydrogenase Content and Maturation
by: Pier Francesco Di Leonardo, et al.
Published: (2022-08-01)