Volume 47, Issue 11 pp. 2052-2054
Communication

Hydrogen-Activating Enzymes: Activity Does Not Correlate with Oxygen Sensitivity

Carole Baffert Dr.

Carole Baffert Dr.

Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Université de Provence, Marseille, France, Fax: (+33) 4-9116-4578 http://bip.cnrs-mrs.fr/bip06/

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Marie Demuez Dr.

Marie Demuez Dr.

Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés, CNRS, INRA, INSA, Toulouse, France

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Laurent Cournac Dr.

Laurent Cournac Dr.

Laboratoire de Bioénergétique et Biotechnologie des Bactéries et Microalgues, CEA, DSV, IBEB, CNRS, Univ. Aix Marseille II, St Paul-lez-Durance, France

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Bénédicte Burlat Dr.

Bénédicte Burlat Dr.

Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Université de Provence, Marseille, France, Fax: (+33) 4-9116-4578 http://bip.cnrs-mrs.fr/bip06/

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Bruno Guigliarelli Prof.

Bruno Guigliarelli Prof.

Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Université de Provence, Marseille, France, Fax: (+33) 4-9116-4578 http://bip.cnrs-mrs.fr/bip06/

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Patrick Bertrand Prof.

Patrick Bertrand Prof.

Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Université de Provence, Marseille, France, Fax: (+33) 4-9116-4578 http://bip.cnrs-mrs.fr/bip06/

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Laurence Girbal Dr.

Laurence Girbal Dr.

Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés, CNRS, INRA, INSA, Toulouse, France

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Christophe Léger Dr.

Christophe Léger Dr.

Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Université de Provence, Marseille, France, Fax: (+33) 4-9116-4578 http://bip.cnrs-mrs.fr/bip06/

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First published: 22 February 2008
Citations: 85

We acknowledge Sébastien Dementin for help and fruitful discussions, funding from the ANR, and support from the Pôle de Compétitivité Capénergies.

Graphical Abstract

Surprisingly uninhibited: The inhibition of hydrogenases by oxygen is intensely studied because this is the main obstacle to using these enzymes in biofuel cells. The hydrogenase from Clostridium acetobutylicum (see structure) was found to react surprisingly slowly with O2. The inhibition mechanism was elucidated and the kinetics were quantitatively defined. This is a prerequisite for improving the enzyme further by genetic engineering and for assessing its potential in technological devices.

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