Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases | Zendy

Lindsey A. Flanagan | Zendy; Alison Parkin | Zendy

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Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases

Author(s) -

Lindsey A. Flanagan,

Alison Parkin

Publication year - 2016

Publication title -

biochemical society transactions

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.562

H-Index - 144

eISSN - 1470-8752

pISSN - 0300-5127

DOI - 10.1042/bst20150201

Subject(s) - hydrogenase , bimetallic strip , electrochemistry , reactivity (psychology) , chemistry , electron transfer , active site , catalysis , enzyme , redox , membrane , combinatorial chemistry , inorganic chemistry , electrode , photochemistry , biochemistry , medicine , alternative medicine , pathology

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.

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