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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.

SUBMITTER: Flanagan LA

PROVIDER: S-EPMC4747160 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature

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Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases.

Flanagan Lindsey A LA Parkin Alison A

Biochemical Society transactions 20160201 1

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 c ...[more]

PMID: 26862221

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