Gated electron transfer of cytochrome c6at biomimetic interfaces: a time-resolved SERR studyElectronic supplementary information (ESI) available: RR spectral parameters and kinetic simulations. See DOI: 10.1039/b904434e.

Bibliographic Details
Title: Gated electron transfer of cytochrome c6at biomimetic interfaces: a time-resolved SERR studyElectronic supplementary information (ESI) available: RR spectral parameters and kinetic simulations. See DOI: 10.1039/b904434e.
Authors: Anja Kranich, Hendrik Naumann, Fernando P. Molina-Heredia, H. Justin Moore, T. Randall Lee, Sophie Lecomte, Miguel A. de la Rosa, Peter Hildebrandt, Daniel H. Murgida
Source: Physical Chemistry Chemical Physics (PCCP); 9/14/2009, Vol. 11 Issue 34, p7390-7397, 8p
Abstract: The electron shuttle heme protein Cyt-c6from the photosynthetic cyanobacterium Nostocsp. 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-c6complexes 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. [ABSTRACT FROM AUTHOR]
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Database: Complementary Index
More Details
ISSN:14639076
DOI:10.1039/b904434e
Published in:Physical Chemistry Chemical Physics (PCCP)
Language:English