Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c

Autores
Álvarez Paggi, Damián Jorge; Castro, Maria Ana; Tortora, Verónica; Castro, Laura; Radi, Rafael; Murgida, Daniel Horacio
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein–protein and protein–lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first- (M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer.
Fil: Álvarez Paggi, Damián Jorge. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
Fil: Castro, Maria Ana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
Fil: Tortora, Verónica. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Castro, Laura. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Radi, Rafael. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Murgida, Daniel Horacio. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
Materia
Cytochrome C
Electron Transfer
Reorganization Energy
Electrostatic Switch
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:11336/757
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/757
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome cÁlvarez Paggi, Damián JorgeCastro, Maria AnaTortora, VerónicaCastro, LauraRadi, RafaelMurgida, Daniel HoracioCytochrome CElectron TransferReorganization EnergyElectrostatic Switchhttps://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.4We have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein–protein and protein–lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first- (M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer.Fil: Álvarez Paggi, Damián Jorge. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;Fil: Castro, Maria Ana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;Fil: Tortora, Verónica. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;Fil: Castro, Laura. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;Fil: Radi, Rafael. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;Fil: Murgida, Daniel Horacio. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;Amer Chemical Soc2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/757Álvarez Paggi, Damián Jorge; Castro, Maria Ana; Tortora, Verónica; Castro, Laura; Radi, Rafael; et al.; Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c; Amer Chemical Soc; Journal of the American Chemical Society; 135; 3-2013; 4389-43970002-7863enginfo:eu-repo/semantics/altIdentifier/doi/10.1021/ja311786binfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ja311786binfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:09:12Zoai:ri.conicet.gov.ar:11336/757instacron: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:34982025-10-22 11:09:12.564CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
title Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
spellingShingle Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
Álvarez Paggi, Damián Jorge
Cytochrome C
Electron Transfer
Reorganization Energy
Electrostatic Switch
title_short Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
title_full Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
title_fullStr Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
title_full_unstemmed Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
title_sort Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c
dc.creator.none.fl_str_mv Álvarez Paggi, Damián Jorge
Castro, Maria Ana
Tortora, Verónica
Castro, Laura
Radi, Rafael
Murgida, Daniel Horacio
author Álvarez Paggi, Damián Jorge
author_facet Álvarez Paggi, Damián Jorge
Castro, Maria Ana
Tortora, Verónica
Castro, Laura
Radi, Rafael
Murgida, Daniel Horacio
author_role author
author2 Castro, Maria Ana
Tortora, Verónica
Castro, Laura
Radi, Rafael
Murgida, Daniel Horacio
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Cytochrome C
Electron Transfer
Reorganization Energy
Electrostatic Switch
topic Cytochrome C
Electron Transfer
Reorganization Energy
Electrostatic Switch
purl_subject.fl_str_mv https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.4
dc.description.none.fl_txt_mv We have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein–protein and protein–lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first- (M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer.
Fil: Álvarez Paggi, Damián Jorge. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
Fil: Castro, Maria Ana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
Fil: Tortora, Verónica. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Castro, Laura. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Radi, Rafael. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;
Fil: Murgida, Daniel Horacio. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;
description We have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein–protein and protein–lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first- (M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer.
publishDate 2013
dc.date.none.fl_str_mv 2013-03
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/11336/757
Álvarez Paggi, Damián Jorge; Castro, Maria Ana; Tortora, Verónica; Castro, Laura; Radi, Rafael; et al.; Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c; Amer Chemical Soc; Journal of the American Chemical Society; 135; 3-2013; 4389-4397
0002-7863
url http://hdl.handle.net/11336/757
identifier_str_mv Álvarez Paggi, Damián Jorge; Castro, Maria Ana; Tortora, Verónica; Castro, Laura; Radi, Rafael; et al.; Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c; Amer Chemical Soc; Journal of the American Chemical Society; 135; 3-2013; 4389-4397
0002-7863
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/ja311786b
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ja311786b
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 Amer Chemical Soc
publisher.none.fl_str_mv Amer Chemical Soc
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
_version_ 1846781432951734272
score 12.982451

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