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Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
Citation key ISI:000269082000007
Author 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.
Pages 7390-7397
Year 2009
ISSN 1463-9076
DOI 10.1039/b904434e
Address THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Journal Phys. chem. chem. phys.
Volume 11
Number 34
Publisher ROYAL SOC CHEMISTRY
Abstract 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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