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Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
Zitatschlüssel ISI:000269082000007
Autor Kranich, Anja and Naumann, Hendrik and Molina-Heredia, Fernando P. and Moore, H. Justin and Lee, T. Randall and Lecomte, Sophie and de la Rosa, Miguel A. and Hildebrandt, Peter and Murgida, Daniel H.
Seiten 7390-7397
Jahr 2009
ISSN 1463-9076
DOI 10.1039/b904434e
Adresse THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Journal Phys. chem. chem. phys.
Jahrgang 11
Nummer 34
Verlag ROYAL SOC CHEMISTRY
Zusammenfassung The electron shuttle heme protein Cyt-c(6) from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c(6) complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.
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