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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).