Skip to Main content Skip to Navigation
Journal articles

Electrochemical measurements of the kinetics of inhibition of two FeFe hydrogenases by O2 demonstrate that the reaction is partly reversible

Abstract : The mechanism of reaction of FeFe hydrogenases with oxygen has been debated. It is complex, apparently very dependent on the details of the protein structure, and difficult to study using conventional kinetic techniques. Here we build on our recent work on the anaerobic inactivation of the enzyme [Fourmond et al, Nat. Chem. 4 336 (2014)] to propose and apply a new method for studying this reaction. Using electrochemical measurements of the turnover rate of hydrogenase, we could resolve the first steps of the inhibition reaction and accurately determine their rates. We show that the two most studied FeFe hydrogenases, from Chlamydomonas reinhardtii and Clostridium acetobutylicum, react with O2 according to the same mechanism, despite the fact that the former is much more O2 sensitive than the latter. Unlike often assumed, both enzymes are reversibly inhibited by a short exposure to O2. This will have to be considered to elucidate the mechanism of inhibition, before any prediction can be made regarding which mutations will improve oxygen resistance. We hope that the approach described herein will prove useful in this respect.
Document type :
Journal articles
Complete list of metadatas

Cited literature [18 references]  Display  Hide  Download

https://hal.archives-ouvertes.fr/hal-01211469
Contributor : Christophe Léger <>
Submitted on : Monday, October 5, 2015 - 11:06:31 AM
Last modification on : Thursday, May 28, 2020 - 3:33:22 AM
Document(s) archivé(s) le : Wednesday, January 6, 2016 - 10:32:28 AM

File

orain-revised-10.1021-jacs.5b0...
Files produced by the author(s)

Identifiers

Citation

Christophe Orain, Laure Saujet, Charles Gauquelin, Philippe Soucaille, Isabelle Meynial Salles, et al.. Electrochemical measurements of the kinetics of inhibition of two FeFe hydrogenases by O2 demonstrate that the reaction is partly reversible. Journal of the American Chemical Society, American Chemical Society, 2015, 137 (39), pp.12580-12587. ⟨10.1021/jacs.5b06934⟩. ⟨hal-01211469⟩

Share

Metrics

Record views

592

Files downloads

459