title: Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases.
abstract: Hydrogenases are enzymes of great biotechnological relevance because they catalyse the interconversion of H2, water (protons) and electricity using non-precious metal catalytic active sites. Electrochemical studies into the reactivity of NiFe membrane-bound hydrogenases (MBH) have provided a particularly detailed insight into the reactivity and mechanism of this group of enzymes. Significantly, the control centre for enabling O2 tolerance has been revealed as the electron-transfer relay of FeS clusters, rather than the NiFe bimetallic active site. The present review paper will discuss how electrochemistry results have complemented those obtained from structural and spectroscopic studies, to present a complete picture of our current understanding of NiFe MBH.
authors: Department of Chemistry, University of York, Heslington, York YO10 5DD, U.K.
authors: Lindsey A
authors: LA
authors: Flanagan
authors: Department of Chemistry, University of York, Heslington, York YO10 5DD, U.K. 2013 Early Career Research Award, Theme Panel III Energy and Metabolism alison.parkin@york.ac.uk.
authors: Alison
authors: A
authors: Parkin
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D002462:Cell Membrane / Q000201:enzymology*; D004563:Electrochemistry; D004579:Electron Transport; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data
chemical_list: C043296:nickel-iron hydrogenase; D006864:Hydrogenase
keywords: NiFe hydrogenase; iron–sulfur cluster relay; membrane-bound hydrogenase; oxygen tolerance; protein film electrochemistry