Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study

The electron shuttle heme protein Cyt-c6 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...

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Detalles Bibliográficos
Autores principales: Kranich, A., Naumann, H., Molina-Heredia, F.P., Moore, H.J., Lee, T.R., Lecomte, S., De La Rosa, M.A., Hildebrandt, P., Murgida, D.H.
Formato: JOUR
Materias:
cytochrome c6
article
binding site
biological model
biomimetics
chemistry
electron
enzymology
genetics
kinetics
mutation
Nostoc
Raman spectrometry
surface property
Binding Sites
Biomimetics
Cytochromes c6
Electrons
Kinetics
Models, Biological
Mutation
Spectrum Analysis, Raman
Surface Properties
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_14639076_v11_n34_p7390_Kranich
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:The electron shuttle heme protein Cyt-c6 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-c6 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. © 2009 the Owner Societies.

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