Financial support by Région Provence-Alpes-Côte d’Azur, Programme Interdisciplinaire Energie CNRS and ANR Bioénergie. We thank Dr. A. Ronda and NanoTecMat technological facility for atomic force microscopy (AFM) experiments, Dr. S. Canaan and S. Robert for TLC experiments, and M. Bauzan for growing the bacteria. PM-IRRA=polarization modulation infrared reflection adsorption.
Electrochemistry, AFM, and PM-IRRA Spectroscopy of Immobilized Hydrogenase: Role of a Hydrophobic Helix in Enzyme Orientation for Efficient H2 Oxidation†
Article first published online: 15 DEC 2011
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 4, pages 953–956, January 23, 2012
How to Cite
Ciaccafava, A., Infossi, P., Ilbert, M., Guiral, M., Lecomte, S., Giudici-Orticoni, M. T. and Lojou, E. (2012), Electrochemistry, AFM, and PM-IRRA Spectroscopy of Immobilized Hydrogenase: Role of a Hydrophobic Helix in Enzyme Orientation for Efficient H2 Oxidation. Angew. Chem. Int. Ed., 51: 953–956. doi: 10.1002/anie.201107053
- Issue published online: 17 JAN 2012
- Article first published online: 15 DEC 2011
- Manuscript Received: 5 OCT 2011
- Région Provence-Alpes-Côte d’Azur
- ANR Bioénergie
- IR spectroscopy;
- membrane protein;
A transmembrane helix surrounded by detergent molecules close to the surface electron relay is shown, by electrochemical, AFM, and PM-IRRAS studies, to control the orientation of a membrane-bound [NiFe] hydrogenase on electrochemical interfaces. Hence, H2 oxidation proceeds as a mixture of direct (DET) and mediated electron transfer (MET) on hydrophilic interfaces, but by a MET process on hydrophobic interfaces (see picture).