Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 13, Pages 4848-4857Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja910685j
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Funding
- CNRS
- CEA
- ANR
- Aix-Marseille Universite
- City of Marseilles
- pole de competitivite Capenergies
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Hydrogenases catalyze the oxidation and production of H-2. The fact that they could be used in biotechnological devices if they resisted inhibition by O-2 motivates the current research on their inactivation mechanism. Direct electrochemistry has been thoroughly used in this respect but often in a qualitative manner. We propose a new and precise chronoamperometric method for studying the anaerobic inactivation mechanism of hydrogenase, which we apply to the oxygen-tolerant NiFe enzyme from Aquifex aeolicus. We demonstrate that the voltammetric data cannot be used for measuring the reduction potential of the so-called NiB inactive state, even in the small scan rate limit. We show that the inactivation mechanism proposed for standard (oxygen-sensitive) NiFe hydrogenases does not apply in the case of the enzyme from A. aeolicus. In particular, the activation and inactivation reactions cannot follow the same reaction pathway.
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