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

Volumn 51, Issue 4, 2012, Pages 953-956

  Ciaccafava, Alexandre ^a   Infossi, Pascale ^a   Ilbert, Marianne ^a   Guiral, Marianne ^a   Lecomte, Sophie ^b   Giudici Orticoni, Marie Thér̀se ^a   Lojou, Elisabeth ^a  

^a CNRS   (France)

^b CNRS   (France)

Author keywords

electrochemistry; enzymes; IR spectroscopy; membrane protein; monolayers

Indexed keywords

[NIFE]-HYDROGENASE; AFM; DETERGENT MOLECULES; ELECTROCHEMICAL INTERFACE; HYDROGENASES; HYDROPHILIC INTERFACES; HYDROPHOBIC HELIX; HYDROPHOBIC INTERFACE; MEDIATED ELECTRON TRANSFER; MEMBRANE PROTEIN; MEMBRANE-BOUND; PM-IRRAS; SURFACE ELECTRON; TRANSMEMBRANE HELICES;

BIOLOGICAL MEMBRANES; ENZYMES; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MONOLAYERS;

ELECTROCHEMISTRY;

DODECYL MALTOSIDE; GLUCOSIDE; GOLD; HYDROGENASE; IMMOBILIZED ENZYME; NICKEL IRON HYDROGENASE; NICKEL-IRON HYDROGENASE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CHEMICAL PHENOMENA; CHEMISTRY; ELECTROCHEMICAL ANALYSIS; ELECTRODE; ENZYME ACTIVE SITE; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN SECONDARY STRUCTURE;

CATALYTIC DOMAIN; ELECTROCHEMICAL TECHNIQUES; ELECTRODES; ENZYMES, IMMOBILIZED; GLUCOSIDES; GOLD; HYDROGENASE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICROSCOPY, ATOMIC FORCE; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY;

EID: 84856012471     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201107053     Document Type: Article

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