Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases
| Autor: | Lindsey A, Flanagan, Alison, Parkin |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
membrane-bound hydrogenase
oxygen tolerance Cell Membrane Molecular Sequence Data Bioenergetics in Mitochondria Bacteria and Chloroplasts Models Biological S4 Electron Transport Hydrogenase Catalytic Domain Electrochemistry Amino Acid Sequence Biochemical Society Focused Meetings iron–sulfur cluster relay NiFe hydrogenase protein film electrochemistry |
| Zdroj: | Biochemical Society Transactions |
| ISSN: | 1470-8752 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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