Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation

Autores
Álvarez Paggi, Damián Jorge; Meister, Wiebke; Kuhlmann, Uwe; Weidinger, Inez; Tenger, Katalin; Zimányi, Lázló; Rákhely, Gabor; Hildebrandt , Peter; Murgida, Daniel Horacio
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Non-exponential distance-dependence of the apparent electron transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behaviour may arise from the structural and dynamical complexity not only of the redox proteins, but also from their interplay with strong electric fields present in the experimental setups and in vivo (J. Am Chem. Soc 2010, 132, 5769-5778). Therefore, protein dynamics are finely controlled by the energetics of both specific contacts and the interaction between the protein?s dipole moment and the interfacial electric fields. In turn, protein dynamics may govern electron transfer kinetics through reorientation from low to high donor-acceptor electronic coupling orientations. Here we present a combined computational and experimental study of WT cytochrome c and the surface mutant K87C adsorbed on electrodes coated with self assembled monolayers (SAMs) of varying thickness (i.e., variable strength of the interfacial electric field). Replacement of the positively charged K87 by a neutral amino acid allowed us to disentangle protein dynamics and electron tunnelling from the reaction kinetics and to rationalize the anomalous distance dependence in terms of (at least) two populations of distinct average electronic couplings. Thus, it was possible to recover the exponential distance dependence expected from ET theory. These results pave the way for gaining further insight into the parameters that control protein electron transfer.
Fil: Álvarez Paggi, Damián Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Meister, Wiebke. Technishe Universitat Berlin; Alemania
Fil: Kuhlmann, Uwe. Technishe Universitat Berlin; Alemania
Fil: Weidinger, Inez. Technishe Universitat Berlin; Alemania
Fil: Tenger, Katalin. Biological Research Center; Hungría
Fil: Zimányi, Lázló. Biological Research Center; Hungría
Fil: Rákhely, Gabor. University Of Szeged. Department of Biotechnology; Hungría
Fil: Hildebrandt , Peter. 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; Argentina. Universidad de Buenos Aires; Argentina
Materia
Transferencia Electrónica
Serr
Pathways
Citocromo
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:11336/8020
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/8020
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface MutationÁlvarez Paggi, Damián JorgeMeister, WiebkeKuhlmann, UweWeidinger, InezTenger, KatalinZimányi, LázlóRákhely, GaborHildebrandt , PeterMurgida, Daniel HoracioTransferencia ElectrónicaSerrPathwaysCitocromohttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Non-exponential distance-dependence of the apparent electron transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behaviour may arise from the structural and dynamical complexity not only of the redox proteins, but also from their interplay with strong electric fields present in the experimental setups and in vivo (J. Am Chem. Soc 2010, 132, 5769-5778). Therefore, protein dynamics are finely controlled by the energetics of both specific contacts and the interaction between the protein?s dipole moment and the interfacial electric fields. In turn, protein dynamics may govern electron transfer kinetics through reorientation from low to high donor-acceptor electronic coupling orientations. Here we present a combined computational and experimental study of WT cytochrome c and the surface mutant K87C adsorbed on electrodes coated with self assembled monolayers (SAMs) of varying thickness (i.e., variable strength of the interfacial electric field). Replacement of the positively charged K87 by a neutral amino acid allowed us to disentangle protein dynamics and electron tunnelling from the reaction kinetics and to rationalize the anomalous distance dependence in terms of (at least) two populations of distinct average electronic couplings. Thus, it was possible to recover the exponential distance dependence expected from ET theory. These results pave the way for gaining further insight into the parameters that control protein electron transfer.Fil: Álvarez Paggi, Damián Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; ArgentinaFil: Meister, Wiebke. Technishe Universitat Berlin; AlemaniaFil: Kuhlmann, Uwe. Technishe Universitat Berlin; AlemaniaFil: Weidinger, Inez. Technishe Universitat Berlin; AlemaniaFil: Tenger, Katalin. Biological Research Center; HungríaFil: Zimányi, Lázló. Biological Research Center; HungríaFil: Rákhely, Gabor. University Of Szeged. Department of Biotechnology; HungríaFil: Hildebrandt , Peter. 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; Argentina. Universidad de Buenos Aires; ArgentinaAmerican Chemical Society2013-04-23info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8020Álvarez Paggi, Damián Jorge; Meister, Wiebke; Kuhlmann, Uwe; Weidinger, Inez; Tenger, Katalin; et al.; Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation; American Chemical Society; Journal Of Physical Chemistry B; 117; 20; 23-4-2013; 6061-60681089-5647enginfo:eu-repo/semantics/altIdentifier/doi/10.1021/jp400832minfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/jp400832minfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:16Zoai:ri.conicet.gov.ar:11336/8020instacron: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 12:00:17.056CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
title Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
spellingShingle Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
Álvarez Paggi, Damián Jorge
Transferencia Electrónica
Serr
Pathways
Citocromo
title_short Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
title_full Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
title_fullStr Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
title_full_unstemmed Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
title_sort Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation
dc.creator.none.fl_str_mv Álvarez Paggi, Damián Jorge
Meister, Wiebke
Kuhlmann, Uwe
Weidinger, Inez
Tenger, Katalin
Zimányi, Lázló
Rákhely, Gabor
Hildebrandt , Peter
Murgida, Daniel Horacio
author Álvarez Paggi, Damián Jorge
author_facet Álvarez Paggi, Damián Jorge
Meister, Wiebke
Kuhlmann, Uwe
Weidinger, Inez
Tenger, Katalin
Zimányi, Lázló
Rákhely, Gabor
Hildebrandt , Peter
Murgida, Daniel Horacio
author_role author
author2 Meister, Wiebke
Kuhlmann, Uwe
Weidinger, Inez
Tenger, Katalin
Zimányi, Lázló
Rákhely, Gabor
Hildebrandt , Peter
Murgida, Daniel Horacio
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Transferencia Electrónica
Serr
Pathways
Citocromo
topic Transferencia Electrónica
Serr
Pathways
Citocromo
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Non-exponential distance-dependence of the apparent electron transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behaviour may arise from the structural and dynamical complexity not only of the redox proteins, but also from their interplay with strong electric fields present in the experimental setups and in vivo (J. Am Chem. Soc 2010, 132, 5769-5778). Therefore, protein dynamics are finely controlled by the energetics of both specific contacts and the interaction between the protein?s dipole moment and the interfacial electric fields. In turn, protein dynamics may govern electron transfer kinetics through reorientation from low to high donor-acceptor electronic coupling orientations. Here we present a combined computational and experimental study of WT cytochrome c and the surface mutant K87C adsorbed on electrodes coated with self assembled monolayers (SAMs) of varying thickness (i.e., variable strength of the interfacial electric field). Replacement of the positively charged K87 by a neutral amino acid allowed us to disentangle protein dynamics and electron tunnelling from the reaction kinetics and to rationalize the anomalous distance dependence in terms of (at least) two populations of distinct average electronic couplings. Thus, it was possible to recover the exponential distance dependence expected from ET theory. These results pave the way for gaining further insight into the parameters that control protein electron transfer.
Fil: Álvarez Paggi, Damián Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Meister, Wiebke. Technishe Universitat Berlin; Alemania
Fil: Kuhlmann, Uwe. Technishe Universitat Berlin; Alemania
Fil: Weidinger, Inez. Technishe Universitat Berlin; Alemania
Fil: Tenger, Katalin. Biological Research Center; Hungría
Fil: Zimányi, Lázló. Biological Research Center; Hungría
Fil: Rákhely, Gabor. University Of Szeged. Department of Biotechnology; Hungría
Fil: Hildebrandt , Peter. 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; Argentina. Universidad de Buenos Aires; Argentina
description Non-exponential distance-dependence of the apparent electron transfer (ET) rate has been reported for a variety of redox proteins immobilized on biocompatible electrodes, thus posing a physicochemical challenge of possible physiological relevance. We have recently proposed that this behaviour may arise from the structural and dynamical complexity not only of the redox proteins, but also from their interplay with strong electric fields present in the experimental setups and in vivo (J. Am Chem. Soc 2010, 132, 5769-5778). Therefore, protein dynamics are finely controlled by the energetics of both specific contacts and the interaction between the protein?s dipole moment and the interfacial electric fields. In turn, protein dynamics may govern electron transfer kinetics through reorientation from low to high donor-acceptor electronic coupling orientations. Here we present a combined computational and experimental study of WT cytochrome c and the surface mutant K87C adsorbed on electrodes coated with self assembled monolayers (SAMs) of varying thickness (i.e., variable strength of the interfacial electric field). Replacement of the positively charged K87 by a neutral amino acid allowed us to disentangle protein dynamics and electron tunnelling from the reaction kinetics and to rationalize the anomalous distance dependence in terms of (at least) two populations of distinct average electronic couplings. Thus, it was possible to recover the exponential distance dependence expected from ET theory. These results pave the way for gaining further insight into the parameters that control protein electron transfer.
publishDate 2013
dc.date.none.fl_str_mv 2013-04-23
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/11336/8020
Álvarez Paggi, Damián Jorge; Meister, Wiebke; Kuhlmann, Uwe; Weidinger, Inez; Tenger, Katalin; et al.; Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation; American Chemical Society; Journal Of Physical Chemistry B; 117; 20; 23-4-2013; 6061-6068
1089-5647
url http://hdl.handle.net/11336/8020
identifier_str_mv Álvarez Paggi, Damián Jorge; Meister, Wiebke; Kuhlmann, Uwe; Weidinger, Inez; Tenger, Katalin; et al.; Disentangling Electron Tunneling and Protein Dynamics of Cytochrome c Through a Rationally Designed Surface Mutation; American Chemical Society; Journal Of Physical Chemistry B; 117; 20; 23-4-2013; 6061-6068
1089-5647
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/jp400832m
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/jp400832m
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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 12.982451

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