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...
| Autores principales: | , , , , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_14639076_v11_n34_p7390_Kranich |
| Aporte de: |
| id |
todo:paper_14639076_v11_n34_p7390_Kranich |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_14639076_v11_n34_p7390_Kranich2023-10-03T16:16:43Z Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study 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. 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 Nostoc Spectrum Analysis, Raman Surface Properties 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14639076_v11_n34_p7390_Kranich |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 Nostoc Spectrum Analysis, Raman Surface Properties |
| spellingShingle |
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 Nostoc Spectrum Analysis, Raman Surface Properties 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. Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| topic_facet |
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 Nostoc Spectrum Analysis, Raman Surface Properties |
| description |
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. |
| format |
JOUR |
| author |
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. |
| author_facet |
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. |
| author_sort |
Kranich, A. |
| title |
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| title_short |
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| title_full |
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| title_fullStr |
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| title_full_unstemmed |
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study |
| title_sort |
gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved serr study |
| url |
http://hdl.handle.net/20.500.12110/paper_14639076_v11_n34_p7390_Kranich |
| work_keys_str_mv |
AT kranicha gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT naumannh gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT molinaherediafp gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT moorehj gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT leetr gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT lecomtes gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT delarosama gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT hildebrandtp gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy AT murgidadh gatedelectrontransferofcytochromec6atbiomimeticinterfacesatimeresolvedserrstudy |
| _version_ |
1807319043433037824 |