Enzyme Film Electrochemistry

Butt, Julea N.; Gates, Andrew J.; Marritt, Sophie J.; Richardson, David J.

doi:10.1002/9781118899076.ch5

Cited by 1 publication

(1 citation statement)

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“…The lack of consensus in determining exactly what active site structure is generated when O 2 sensitive NiFe hydrogenases react with O 2 may be in part attributable to the fact that O 2 inactivation can also generate “dead” states of permanently inactivated enzyme [ 19 ]. In electrochemistry it is difficult to separate an estimate of dead phase formation from “film loss”, the normal steady drop in enzyme activity which is observed over long experiments and is probably due to desorption of enzyme from the electrode [ 56 ]. If the hydrogenase dead phase is non-paramagnetic then it will also be rendered spectroscopically silent via EPR, and small numbers of molecules are hard to detect using FTIR.…”

Section: Active Site Statesmentioning

confidence: 99%

Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases

Flanagan

Parkin

2016

Biochemical Society Transactions

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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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Section: Active Site Statesmentioning

confidence: 99%