Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c

Autores
Khoa Ly, H.; Wisitruangsakul, Nattawadee; Sezer, Murat; Feng, Jiu-Ju; Kranich, Anja; Weidinger, Inez M.; Zebger, Ingo; Murgida, Daniel Horacio; Hildebrandt, Peter
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Time-resolved surface enhanced resonance Raman and surface enhanced infrared absorption spectroscopy have been employed to study the interfacial redox process of cytochrome c (Cyt-c) immobilised on various metal electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated mercaptanes. The experiments, carried out with Ag, Au and layered Au-SAM-Ag electrodes, afford apparent heterogeneous electron transfer constants (krelax) that reflect the interplay between electron tunnelling, redox-linked protein structural changes, protein re-orientation, and hydrogen bond re-arrangements in the protein and in the protein/SAM interface. It is shown that the individual processes are affected by the interfacial electric field strength that increases with decreasing thickness of the SAM and increasing difference between the actual potential and the potential of zero-charge. At thick SAMs of mercaptanes including 15 methylene groups, electron tunnelling (kET) is the rate-limiting step. Pronounced differences for kET and its overpotential-dependence are observed for the three metal electrodes and can be attributed to the different electric-field effects on the free-energy term controlling the tunnelling rate. With decreasing SAM thickness, electron tunnelling increases whereas protein dynamics is slowed down such that for SAMs including less than 10 methylene groups, protein re-orientation becomes rate-limiting, as reflected by the viscosity dependence of krelax. Upon decreasing the SAM thickness from 5 to 1 methylene group, an additional H/D kinetic isotope effect is detected indicating that at very high electric fields re-arrangements of the interfacial or intra-protein hydrogen bond networks limit the rate of the overall redox process.
Fil: Khoa Ly, H.. Technishe Universitat Berlin; Alemania
Fil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; Tailandia
Fil: Sezer, Murat. Technishe Universitat Berlin; Alemania
Fil: Feng, Jiu-Ju. Henan Normal University; China. Technishe Universitat Berlin; Alemania
Fil: Kranich, Anja. Technishe Universitat Berlin; Alemania
Fil: Weidinger, Inez M.. Technishe Universitat Berlin; Alemania
Fil: Zebger, Ingo. Technishe Universitat Berlin; Alemania
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
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
Materia
Cytochrome C
Electric Field
Electron Transfer
Surface Enhanced Infrared Spectroscopy
Surface Enhanced Raman Spectroscopy
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/68711
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/68711
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome cKhoa Ly, H.Wisitruangsakul, NattawadeeSezer, MuratFeng, Jiu-JuKranich, AnjaWeidinger, Inez M.Zebger, IngoMurgida, Daniel HoracioHildebrandt, PeterCytochrome CElectric FieldElectron TransferSurface Enhanced Infrared SpectroscopySurface Enhanced Raman Spectroscopyhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Time-resolved surface enhanced resonance Raman and surface enhanced infrared absorption spectroscopy have been employed to study the interfacial redox process of cytochrome c (Cyt-c) immobilised on various metal electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated mercaptanes. The experiments, carried out with Ag, Au and layered Au-SAM-Ag electrodes, afford apparent heterogeneous electron transfer constants (krelax) that reflect the interplay between electron tunnelling, redox-linked protein structural changes, protein re-orientation, and hydrogen bond re-arrangements in the protein and in the protein/SAM interface. It is shown that the individual processes are affected by the interfacial electric field strength that increases with decreasing thickness of the SAM and increasing difference between the actual potential and the potential of zero-charge. At thick SAMs of mercaptanes including 15 methylene groups, electron tunnelling (kET) is the rate-limiting step. Pronounced differences for kET and its overpotential-dependence are observed for the three metal electrodes and can be attributed to the different electric-field effects on the free-energy term controlling the tunnelling rate. With decreasing SAM thickness, electron tunnelling increases whereas protein dynamics is slowed down such that for SAMs including less than 10 methylene groups, protein re-orientation becomes rate-limiting, as reflected by the viscosity dependence of krelax. Upon decreasing the SAM thickness from 5 to 1 methylene group, an additional H/D kinetic isotope effect is detected indicating that at very high electric fields re-arrangements of the interfacial or intra-protein hydrogen bond networks limit the rate of the overall redox process.Fil: Khoa Ly, H.. Technishe Universitat Berlin; AlemaniaFil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; TailandiaFil: Sezer, Murat. Technishe Universitat Berlin; AlemaniaFil: Feng, Jiu-Ju. Henan Normal University; China. Technishe Universitat Berlin; AlemaniaFil: Kranich, Anja. Technishe Universitat Berlin; AlemaniaFil: Weidinger, Inez M.. Technishe Universitat Berlin; AlemaniaFil: Zebger, Ingo. Technishe Universitat Berlin; AlemaniaFil: 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; ArgentinaFil: Hildebrandt, Peter. Technishe Universitat Berlin; AlemaniaElsevier Science Sa2011-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/68711Khoa Ly, H.; Wisitruangsakul, Nattawadee; Sezer, Murat; Feng, Jiu-Ju; Kranich, Anja; et al.; Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c; Elsevier Science Sa; Journal of Electroanalytical Chemistry; 660; 2; 9-2011; 367-3761572-66571873-2569CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1572665710005357info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jelechem.2010.12.020info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:12:57Zoai:ri.conicet.gov.ar:11336/68711instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:12:58.22CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
title Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
spellingShingle Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
Khoa Ly, H.
Cytochrome C
Electric Field
Electron Transfer
Surface Enhanced Infrared Spectroscopy
Surface Enhanced Raman Spectroscopy
title_short Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
title_full Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
title_fullStr Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
title_full_unstemmed Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
title_sort Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c
dc.creator.none.fl_str_mv Khoa Ly, H.
Wisitruangsakul, Nattawadee
Sezer, Murat
Feng, Jiu-Ju
Kranich, Anja
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author Khoa Ly, H.
author_facet Khoa Ly, H.
Wisitruangsakul, Nattawadee
Sezer, Murat
Feng, Jiu-Ju
Kranich, Anja
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author_role author
author2 Wisitruangsakul, Nattawadee
Sezer, Murat
Feng, Jiu-Ju
Kranich, Anja
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cytochrome C
Electric Field
Electron Transfer
Surface Enhanced Infrared Spectroscopy
Surface Enhanced Raman Spectroscopy
topic Cytochrome C
Electric Field
Electron Transfer
Surface Enhanced Infrared Spectroscopy
Surface Enhanced Raman Spectroscopy
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Time-resolved surface enhanced resonance Raman and surface enhanced infrared absorption spectroscopy have been employed to study the interfacial redox process of cytochrome c (Cyt-c) immobilised on various metal electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated mercaptanes. The experiments, carried out with Ag, Au and layered Au-SAM-Ag electrodes, afford apparent heterogeneous electron transfer constants (krelax) that reflect the interplay between electron tunnelling, redox-linked protein structural changes, protein re-orientation, and hydrogen bond re-arrangements in the protein and in the protein/SAM interface. It is shown that the individual processes are affected by the interfacial electric field strength that increases with decreasing thickness of the SAM and increasing difference between the actual potential and the potential of zero-charge. At thick SAMs of mercaptanes including 15 methylene groups, electron tunnelling (kET) is the rate-limiting step. Pronounced differences for kET and its overpotential-dependence are observed for the three metal electrodes and can be attributed to the different electric-field effects on the free-energy term controlling the tunnelling rate. With decreasing SAM thickness, electron tunnelling increases whereas protein dynamics is slowed down such that for SAMs including less than 10 methylene groups, protein re-orientation becomes rate-limiting, as reflected by the viscosity dependence of krelax. Upon decreasing the SAM thickness from 5 to 1 methylene group, an additional H/D kinetic isotope effect is detected indicating that at very high electric fields re-arrangements of the interfacial or intra-protein hydrogen bond networks limit the rate of the overall redox process.
Fil: Khoa Ly, H.. Technishe Universitat Berlin; Alemania
Fil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; Tailandia
Fil: Sezer, Murat. Technishe Universitat Berlin; Alemania
Fil: Feng, Jiu-Ju. Henan Normal University; China. Technishe Universitat Berlin; Alemania
Fil: Kranich, Anja. Technishe Universitat Berlin; Alemania
Fil: Weidinger, Inez M.. Technishe Universitat Berlin; Alemania
Fil: Zebger, Ingo. Technishe Universitat Berlin; Alemania
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
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
description Time-resolved surface enhanced resonance Raman and surface enhanced infrared absorption spectroscopy have been employed to study the interfacial redox process of cytochrome c (Cyt-c) immobilised on various metal electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated mercaptanes. The experiments, carried out with Ag, Au and layered Au-SAM-Ag electrodes, afford apparent heterogeneous electron transfer constants (krelax) that reflect the interplay between electron tunnelling, redox-linked protein structural changes, protein re-orientation, and hydrogen bond re-arrangements in the protein and in the protein/SAM interface. It is shown that the individual processes are affected by the interfacial electric field strength that increases with decreasing thickness of the SAM and increasing difference between the actual potential and the potential of zero-charge. At thick SAMs of mercaptanes including 15 methylene groups, electron tunnelling (kET) is the rate-limiting step. Pronounced differences for kET and its overpotential-dependence are observed for the three metal electrodes and can be attributed to the different electric-field effects on the free-energy term controlling the tunnelling rate. With decreasing SAM thickness, electron tunnelling increases whereas protein dynamics is slowed down such that for SAMs including less than 10 methylene groups, protein re-orientation becomes rate-limiting, as reflected by the viscosity dependence of krelax. Upon decreasing the SAM thickness from 5 to 1 methylene group, an additional H/D kinetic isotope effect is detected indicating that at very high electric fields re-arrangements of the interfacial or intra-protein hydrogen bond networks limit the rate of the overall redox process.
publishDate 2011
dc.date.none.fl_str_mv 2011-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/68711
Khoa Ly, H.; Wisitruangsakul, Nattawadee; Sezer, Murat; Feng, Jiu-Ju; Kranich, Anja; et al.; Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c; Elsevier Science Sa; Journal of Electroanalytical Chemistry; 660; 2; 9-2011; 367-376
1572-6657
1873-2569
CONICET Digital
CONICET
url http://hdl.handle.net/11336/68711
identifier_str_mv Khoa Ly, H.; Wisitruangsakul, Nattawadee; Sezer, Murat; Feng, Jiu-Ju; Kranich, Anja; et al.; Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c; Elsevier Science Sa; Journal of Electroanalytical Chemistry; 660; 2; 9-2011; 367-376
1572-6657
1873-2569
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1572665710005357
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jelechem.2010.12.020
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Sa
publisher.none.fl_str_mv Elsevier Science Sa
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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