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dc.contributor.author
Kranich, Anja
dc.contributor.author
Naumann, Hendrik
dc.contributor.author
Molina Heredia, Fernando P.
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Moore, H. Justin
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Lee, T. Randall
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Lecomte, Sophie
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Nuñez de la Rosa, Eduardo Miguel
dc.contributor.author
Hildebrandt, Peter
dc.contributor.author
Murgida, Daniel Horacio
dc.date.available
2019-04-29T23:15:37Z
dc.date.issued
2009-12
dc.identifier.citation
Kranich, Anja; Naumann, Hendrik; Molina Heredia, Fernando P.; Moore, H. Justin; Lee, T. Randall; et al.; Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 34; 12-2009; 7390-7397
dc.identifier.issn
1463-9076
dc.identifier.uri
http://hdl.handle.net/11336/75275
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Royal Society of Chemistry
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Citocromos
dc.subject
Redox Proteins
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Raman
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Protein Dynamics
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-27T17:54:18Z
dc.journal.volume
11
dc.journal.number
34
dc.journal.pagination
7390-7397
dc.journal.pais
Reino Unido
dc.description.fil
Fil: Kranich, Anja. Technische Universität Berlin; Alemania
dc.description.fil
Fil: Naumann, Hendrik. Technische Universität Berlin; Alemania
dc.description.fil
Fil: Molina Heredia, Fernando P.. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Moore, H. Justin. University Of Houston; Estados Unidos
dc.description.fil
Fil: Lee, T. Randall. University Of Houston; Estados Unidos
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Fil: Lecomte, Sophie. Universite de Bordeaux; Francia. Centre National de la Recherche Scientifique; Francia
dc.description.fil
Fil: Nuñez de la Rosa, Eduardo Miguel. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania
dc.description.fil
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.journal.title
Physical Chemistry Chemical Physics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1039/b904434e
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2009/CP/b904434e
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