Flanagan, Lindsey A and Parkin, Alison orcid.org/0000-0003-4715-7200 (2016) Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases. Biochemical Society transactions. pp. 315-28. ISSN 1470-8752
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | 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. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 12 Feb 2016 13:49 |
Last Modified: | 01 Dec 2024 01:07 |
Published Version: | https://doi.org/10.1042/BST20150201 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1042/BST20150201 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:95024 |
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