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
Publicado: 2009
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:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v11_n34_p7390_Kranich
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
id paper:paper_14639076_v11_n34_p7390_Kranich
record_format dspace
spelling paper:paper_14639076_v11_n34_p7390_Kranich2023-06-08T16:16:21Z Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study 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. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v11_n34_p7390_Kranich 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
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.
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
publishDate 2009
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v11_n34_p7390_Kranich
http://hdl.handle.net/20.500.12110/paper_14639076_v11_n34_p7390_Kranich
_version_ 1768543246929100800

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