Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of c...

Autores
Khoa Ly, Hong; Sezer, Murat; Wisitruangsakul, Nattawadee; Feng, Jiu-Ju; Kranich, Anja; Millo, Diego; Weidinger, Inez M.; Zebger, Ingo; Murgida, Daniel Horacio; Hildebrandt, Peter
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.
Fil: Khoa Ly, Hong. Technishe Universitat Berlin; Alemania
Fil: Sezer, Murat. Technishe Universitat Berlin; Alemania
Fil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; Tailandia
Fil: Feng, Jiu-Ju. Technishe Universitat Berlin; Alemania. Henan Normal University; China
Fil: Kranich, Anja. Technishe Universitat Berlin; Alemania
Fil: Millo, Diego. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
Materia
APOPTOSIS
CYTOCHROME C
ELECTRIC FIELD
ELECTRON TRANSFER
PROTEIN DYNAMICS
SURFACE-ENHANCED INFRARED SPECTROSCOPY
SURFACE-ENHANCED RESONANCE 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:11336/72003
Acceder
id CONICETDig_9bca70dd073e489dbe62919b6f3292f8
oai_identifier_str oai:ri.conicet.gov.ar:11336/72003
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome cKhoa Ly, HongSezer, MuratWisitruangsakul, NattawadeeFeng, Jiu-JuKranich, AnjaMillo, DiegoWeidinger, Inez M.Zebger, IngoMurgida, Daniel HoracioHildebrandt, PeterAPOPTOSISCYTOCHROME CELECTRIC FIELDELECTRON TRANSFERPROTEIN DYNAMICSSURFACE-ENHANCED INFRARED SPECTROSCOPYSURFACE-ENHANCED RESONANCE RAMAN SPECTROSCOPYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.Fil: Khoa Ly, Hong. Technishe Universitat Berlin; AlemaniaFil: Sezer, Murat. Technishe Universitat Berlin; AlemaniaFil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; TailandiaFil: Feng, Jiu-Ju. Technishe Universitat Berlin; Alemania. Henan Normal University; ChinaFil: Kranich, Anja. Technishe Universitat Berlin; AlemaniaFil: Millo, Diego. 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; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; ArgentinaFil: Hildebrandt, Peter. Technishe Universitat Berlin; AlemaniaWiley Blackwell Publishing, Inc2011-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/72003Khoa Ly, Hong; Sezer, Murat; Wisitruangsakul, Nattawadee; Feng, Jiu-Ju; Kranich, Anja; et al.; Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c; Wiley Blackwell Publishing, Inc; Febs Journal; 278; 9; 5-2011; 1382-13901742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2011.08064.xinfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2011.08064.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:35:33Zoai:ri.conicet.gov.ar:11336/72003instacron: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:34982025-09-29 09:35:34.268CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
title Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
spellingShingle Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
Khoa Ly, Hong
APOPTOSIS
CYTOCHROME C
ELECTRIC FIELD
ELECTRON TRANSFER
PROTEIN DYNAMICS
SURFACE-ENHANCED INFRARED SPECTROSCOPY
SURFACE-ENHANCED RESONANCE RAMAN SPECTROSCOPY
title_short Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
title_full Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
title_fullStr Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
title_full_unstemmed Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
title_sort Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
dc.creator.none.fl_str_mv Khoa Ly, Hong
Sezer, Murat
Wisitruangsakul, Nattawadee
Feng, Jiu-Ju
Kranich, Anja
Millo, Diego
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author Khoa Ly, Hong
author_facet Khoa Ly, Hong
Sezer, Murat
Wisitruangsakul, Nattawadee
Feng, Jiu-Ju
Kranich, Anja
Millo, Diego
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author_role author
author2 Sezer, Murat
Wisitruangsakul, Nattawadee
Feng, Jiu-Ju
Kranich, Anja
Millo, Diego
Weidinger, Inez M.
Zebger, Ingo
Murgida, Daniel Horacio
Hildebrandt, Peter
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv APOPTOSIS
CYTOCHROME C
ELECTRIC FIELD
ELECTRON TRANSFER
PROTEIN DYNAMICS
SURFACE-ENHANCED INFRARED SPECTROSCOPY
SURFACE-ENHANCED RESONANCE RAMAN SPECTROSCOPY
topic APOPTOSIS
CYTOCHROME C
ELECTRIC FIELD
ELECTRON TRANSFER
PROTEIN DYNAMICS
SURFACE-ENHANCED INFRARED SPECTROSCOPY
SURFACE-ENHANCED RESONANCE 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 Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.
Fil: Khoa Ly, Hong. Technishe Universitat Berlin; Alemania
Fil: Sezer, Murat. Technishe Universitat Berlin; Alemania
Fil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; Tailandia
Fil: Feng, Jiu-Ju. Technishe Universitat Berlin; Alemania. Henan Normal University; China
Fil: Kranich, Anja. Technishe Universitat Berlin; Alemania
Fil: Millo, Diego. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
description Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
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/11336/72003
Khoa Ly, Hong; Sezer, Murat; Wisitruangsakul, Nattawadee; Feng, Jiu-Ju; Kranich, Anja; et al.; Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c; Wiley Blackwell Publishing, Inc; Febs Journal; 278; 9; 5-2011; 1382-1390
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/72003
identifier_str_mv Khoa Ly, Hong; Sezer, Murat; Wisitruangsakul, Nattawadee; Feng, Jiu-Ju; Kranich, Anja; et al.; Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c; Wiley Blackwell Publishing, Inc; Febs Journal; 278; 9; 5-2011; 1382-1390
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2011.08064.x
info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2011.08064.x
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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 13.070432

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