Disentangling interfacial redox processes of proteins by SERR spectroscopy

Autores
Murgida, Daniel Horacio; Hildebrandt, Peter
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach forstudying the structure and reaction dynamics of redox proteins immobilized on biocompatibleelectrodes in fundamental and applied sciences. Using this approach it has been recently shownthat electric fields of biologically relevant magnitude are able to influence crucial parameters forthe functioning of a variety of soluble and membrane bound heme proteins. Electric field effectsdiscussed in this tutorial review include modulation of redox potentials, reorganization energies,protein dynamics and redox-linked structural changes.
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. Technische Universitat Berlin; Alemania
Materia
Raman
Redox proteins
Cytochrome
Bioelectrochemistry
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:11336/103598
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Disentangling interfacial redox processes of proteins by SERR spectroscopyMurgida, Daniel HoracioHildebrandt, PeterRamanRedox proteinsCytochromeBioelectrochemistryhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach forstudying the structure and reaction dynamics of redox proteins immobilized on biocompatibleelectrodes in fundamental and applied sciences. Using this approach it has been recently shownthat electric fields of biologically relevant magnitude are able to influence crucial parameters forthe functioning of a variety of soluble and membrane bound heme proteins. Electric field effectsdiscussed in this tutorial review include modulation of redox potentials, reorganization energies,protein dynamics and redox-linked structural changes.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; ArgentinaFil: Hildebrandt, Peter. Technische Universitat Berlin; AlemaniaRoyal Society of Chemistry2008-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/103598Murgida, Daniel Horacio; Hildebrandt, Peter; Disentangling interfacial redox processes of proteins by SERR spectroscopy; Royal Society of Chemistry; Chemical Society Reviews; 37; 5; 12-2008; 937-9450306-0012CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2008/cs/b705976kinfo:eu-repo/semantics/altIdentifier/doi/10.1039/b705976kinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:13:17Zoai:ri.conicet.gov.ar:11336/103598instacron: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:34982025-09-10 13:13:17.301CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Disentangling interfacial redox processes of proteins by SERR spectroscopy
title Disentangling interfacial redox processes of proteins by SERR spectroscopy
spellingShingle Disentangling interfacial redox processes of proteins by SERR spectroscopy
Murgida, Daniel Horacio
Raman
Redox proteins
Cytochrome
Bioelectrochemistry
title_short Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_full Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_fullStr Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_full_unstemmed Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_sort Disentangling interfacial redox processes of proteins by SERR spectroscopy
dc.creator.none.fl_str_mv Murgida, Daniel Horacio
Hildebrandt, Peter
author Murgida, Daniel Horacio
author_facet Murgida, Daniel Horacio
Hildebrandt, Peter
author_role author
author2 Hildebrandt, Peter
author2_role author
dc.subject.none.fl_str_mv Raman
Redox proteins
Cytochrome
Bioelectrochemistry
topic Raman
Redox proteins
Cytochrome
Bioelectrochemistry
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach forstudying the structure and reaction dynamics of redox proteins immobilized on biocompatibleelectrodes in fundamental and applied sciences. Using this approach it has been recently shownthat electric fields of biologically relevant magnitude are able to influence crucial parameters forthe functioning of a variety of soluble and membrane bound heme proteins. Electric field effectsdiscussed in this tutorial review include modulation of redox potentials, reorganization energies,protein dynamics and redox-linked structural changes.
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. Technische Universitat Berlin; Alemania
description Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach forstudying the structure and reaction dynamics of redox proteins immobilized on biocompatibleelectrodes in fundamental and applied sciences. Using this approach it has been recently shownthat electric fields of biologically relevant magnitude are able to influence crucial parameters forthe functioning of a variety of soluble and membrane bound heme proteins. Electric field effectsdiscussed in this tutorial review include modulation of redox potentials, reorganization energies,protein dynamics and redox-linked structural changes.
publishDate 2008
dc.date.none.fl_str_mv 2008-12
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/11336/103598
Murgida, Daniel Horacio; Hildebrandt, Peter; Disentangling interfacial redox processes of proteins by SERR spectroscopy; Royal Society of Chemistry; Chemical Society Reviews; 37; 5; 12-2008; 937-945
0306-0012
CONICET Digital
CONICET
url http://hdl.handle.net/11336/103598
identifier_str_mv Murgida, Daniel Horacio; Hildebrandt, Peter; Disentangling interfacial redox processes of proteins by SERR spectroscopy; Royal Society of Chemistry; Chemical Society Reviews; 37; 5; 12-2008; 937-945
0306-0012
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://pubs.rsc.org/en/content/articlelanding/2008/cs/b705976k
info:eu-repo/semantics/altIdentifier/doi/10.1039/b705976k
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 Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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 12.993085

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