Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases

Lindsey A Flanagan, Alison Parkin

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)315-28
Number of pages14
JournalBiochemical Society transactions
Issue number1
Publication statusPublished - 9 Feb 2016

Bibliographical note

Accepted for Publication: 13/11/2015. © Authors 2016. This content is made available by the publisher under a Creative Commons Attribution Licence. This means that a user may copy, distribute and display the resource providing that they give credit. Users must adhere to the terms of the licence.

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