Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations

Autores
Morgada, Marcos Nicolás; Abriata, Luciano Andres; Zitare, Ulises Alejandro; Álvarez Paggi, Damián Jorge; Murgida, Daniel Horacio; Vila, Alejandro Jose
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The CuA center is a dinuclear copper site that serves as an optimized hub for long-range electron transfer in heme–copper terminal oxidases. Its electronic structure can be described in terms of a σu* ground-state wavefunction with an alternative, less populated ground state of πu symmetry, which is thermally accessible. It is now shown that second-sphere mutations in the CuA containing subunit of Thermus thermophilus ba3 oxidase perturb the electronic structure, which leads to a substantial increase in the population of the πu state, as shown by different spectroscopic methods. This perturbation does not affect the redox potential of the metal site, and despite an increase in the reorganization energy, it is not detrimental to the electron-transfer kinetics. The mutations were achieved by replacing the loops that are involved in protein–protein interactions with cytochrome c, suggesting that transient protein binding could also elicit ground-state switching in the oxidase, which enables alternative electron-transfer pathways.
Fil: Morgada, Marcos Nicolás. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Abriata, Luciano Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Zitare, Ulises Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina
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
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
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
Electron Transfer
Electronic Structure
Metalloproteins
Nmr Spectroscopy
Second-Shell Perturbations
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:11336/8631
Acceder
id CONICETDig_24be9a854be00b68152b065393bad041
oai_identifier_str oai:ri.conicet.gov.ar:11336/8631
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere PerturbationsMorgada, Marcos NicolásAbriata, Luciano AndresZitare, Ulises AlejandroÁlvarez Paggi, Damián JorgeMurgida, Daniel HoracioVila, Alejandro JoseElectron TransferElectronic StructureMetalloproteinsNmr SpectroscopySecond-Shell Perturbationshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The CuA center is a dinuclear copper site that serves as an optimized hub for long-range electron transfer in heme–copper terminal oxidases. Its electronic structure can be described in terms of a σu* ground-state wavefunction with an alternative, less populated ground state of πu symmetry, which is thermally accessible. It is now shown that second-sphere mutations in the CuA containing subunit of Thermus thermophilus ba3 oxidase perturb the electronic structure, which leads to a substantial increase in the population of the πu state, as shown by different spectroscopic methods. This perturbation does not affect the redox potential of the metal site, and despite an increase in the reorganization energy, it is not detrimental to the electron-transfer kinetics. The mutations were achieved by replacing the loops that are involved in protein–protein interactions with cytochrome c, suggesting that transient protein binding could also elicit ground-state switching in the oxidase, which enables alternative electron-transfer pathways.Fil: Morgada, Marcos Nicolás. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Abriata, Luciano Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Zitare, Ulises Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaWiley2014-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8631Morgada, Marcos Nicolás; Abriata, Luciano Andres; Zitare, Ulises Alejandro; Álvarez Paggi, Damián Jorge; Murgida, Daniel Horacio; et al.; Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations; Wiley; Angewandte Chemie; 53; 24; 6-2014; 6188-61921433-78511521-3773enginfo:eu-repo/semantics/altIdentifier/doi/10.1002/anie.201402083info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/anie.201402083/abstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:02:05Zoai:ri.conicet.gov.ar:11336/8631instacron: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 10:02:05.814CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
title Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
spellingShingle Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
Morgada, Marcos Nicolás
Electron Transfer
Electronic Structure
Metalloproteins
Nmr Spectroscopy
Second-Shell Perturbations
title_short Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
title_full Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
title_fullStr Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
title_full_unstemmed Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
title_sort Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations
dc.creator.none.fl_str_mv Morgada, Marcos Nicolás
Abriata, Luciano Andres
Zitare, Ulises Alejandro
Álvarez Paggi, Damián Jorge
Murgida, Daniel Horacio
Vila, Alejandro Jose
author Morgada, Marcos Nicolás
author_facet Morgada, Marcos Nicolás
Abriata, Luciano Andres
Zitare, Ulises Alejandro
Álvarez Paggi, Damián Jorge
Murgida, Daniel Horacio
Vila, Alejandro Jose
author_role author
author2 Abriata, Luciano Andres
Zitare, Ulises Alejandro
Álvarez Paggi, Damián Jorge
Murgida, Daniel Horacio
Vila, Alejandro Jose
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Electron Transfer
Electronic Structure
Metalloproteins
Nmr Spectroscopy
Second-Shell Perturbations
topic Electron Transfer
Electronic Structure
Metalloproteins
Nmr Spectroscopy
Second-Shell Perturbations
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The CuA center is a dinuclear copper site that serves as an optimized hub for long-range electron transfer in heme–copper terminal oxidases. Its electronic structure can be described in terms of a σu* ground-state wavefunction with an alternative, less populated ground state of πu symmetry, which is thermally accessible. It is now shown that second-sphere mutations in the CuA containing subunit of Thermus thermophilus ba3 oxidase perturb the electronic structure, which leads to a substantial increase in the population of the πu state, as shown by different spectroscopic methods. This perturbation does not affect the redox potential of the metal site, and despite an increase in the reorganization energy, it is not detrimental to the electron-transfer kinetics. The mutations were achieved by replacing the loops that are involved in protein–protein interactions with cytochrome c, suggesting that transient protein binding could also elicit ground-state switching in the oxidase, which enables alternative electron-transfer pathways.
Fil: Morgada, Marcos Nicolás. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Abriata, Luciano Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Zitare, Ulises Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina
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
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
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
description The CuA center is a dinuclear copper site that serves as an optimized hub for long-range electron transfer in heme–copper terminal oxidases. Its electronic structure can be described in terms of a σu* ground-state wavefunction with an alternative, less populated ground state of πu symmetry, which is thermally accessible. It is now shown that second-sphere mutations in the CuA containing subunit of Thermus thermophilus ba3 oxidase perturb the electronic structure, which leads to a substantial increase in the population of the πu state, as shown by different spectroscopic methods. This perturbation does not affect the redox potential of the metal site, and despite an increase in the reorganization energy, it is not detrimental to the electron-transfer kinetics. The mutations were achieved by replacing the loops that are involved in protein–protein interactions with cytochrome c, suggesting that transient protein binding could also elicit ground-state switching in the oxidase, which enables alternative electron-transfer pathways.
publishDate 2014
dc.date.none.fl_str_mv 2014-06
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/11336/8631
Morgada, Marcos Nicolás; Abriata, Luciano Andres; Zitare, Ulises Alejandro; Álvarez Paggi, Damián Jorge; Murgida, Daniel Horacio; et al.; Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations; Wiley; Angewandte Chemie; 53; 24; 6-2014; 6188-6192
1433-7851
1521-3773
url http://hdl.handle.net/11336/8631
identifier_str_mv Morgada, Marcos Nicolás; Abriata, Luciano Andres; Zitare, Ulises Alejandro; Álvarez Paggi, Damián Jorge; Murgida, Daniel Horacio; et al.; Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second Sphere Perturbations; Wiley; Angewandte Chemie; 53; 24; 6-2014; 6188-6192
1433-7851
1521-3773
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/anie.201402083
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/anie.201402083/abstract
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
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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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