Electrochemistry, AFM, and PM‐IRRA Spectroscopy of Immobilized Hydrogenase: Role of a Hydrophobic Helix in Enzyme Orientation for Efficient H 2  Oxidation | Zendy

Ciaccafava Alexandre | Zendy; Infossi Pascale | Zendy; Ilbert Marianne | Zendy; Guiral Marianne | Zendy; Lecomte Sophie | Zendy; GiudiciOrticoni Marie Thérèse | Zendy; Lojou Elisabeth | Zendy

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Electrochemistry, AFM, and PM‐IRRA Spectroscopy of Immobilized Hydrogenase: Role of a Hydrophobic Helix in Enzyme Orientation for Efficient H 2 Oxidation

Author(s) -

Ciaccafava Alexandre,

Infossi Pascale,

Ilbert Marianne,

Guiral Marianne,

Lecomte Sophie,

GiudiciOrticoni Marie Thérèse,

Lojou Elisabeth

Publication year - 2012

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201107053

Subject(s) - electrochemistry , hydrogenase , electron transfer , helix (gastropod) , chemistry , molecule , crystallography , photochemistry , enzyme , organic chemistry , electrode , ecology , snail , biology

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, H 2 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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