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Alexandre Ciaccafava, Pascale Infossi, Dr. Marianne Ilbert, Dr. Marianne Guiral, Dr. Sophie Lecomte, Dr. Marie Thérèse Giudici-Orticoni and Dr. Elisabeth Lojou Electrochemistry, AFM, and PM-IRRA Spectroscopy of Immobilized Hydrogenase: Role of a Hydrophobic Helix in Enzyme Orientation for Efficient H2 Oxidation Angewandte Chemie International Edition 51

Version of Record online: 15 DEC 2011 | DOI: 10.1002/anie.201107053

Thumbnail image of graphical abstract

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).

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