Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis

Autores
Grazina, Raquel; Sousa, Patrícia M. Paes de; Brondino, Carlos Dante; Carepo, Marta S. P.; Moura, Isabel; Moura, José J. G.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The redox behaviour of a ferredoxin (Fd) from Desulfovibrio alaskensis was characterized by electrochemistry. The protein was isolated and purified, and showed to be a tetramer containing one [3Fe–4S] and one [4Fe–4S] centre. This ferredoxin has high homology with FdI from Desulfovibrio vulgaris Miyazaki and Hildenborough and FdIII from Desulfovibrio africanus. From differential pulse voltammetry the following signals were identified: [3Fe-4S]+ 1/0 (E0′ = − 158 ± 5 mV); [4Fe–4S]+ 2/+1 (E0′ = − 474 ± 5 mV) and [3Fe–4S]0/− 2 (E0′ = − 660 ± 5 mV). The effect of pH on these signals showed that the reduced [3Fe–4S]0 cluster has a pKʹred′ = 5.1 ± 0.1, the [4Fe–4S]+ 2/+1 centre is pH independent, and the [3Fe–4S]0/−2 reduction is accompanied by the binding of two protons. The ability of the [3Fe–4S]0 cluster to be converted into a new [4Fe–4S] cluster was proven. The redox potential of the original [4Fe–4S] centre showed to be dependent on the formation of the new [4Fe-4S] centre, which results in a positive shift (ca. 70 mV) of the redox potential of the original centre. Being most [Fe–S] proteins involved in electron transport processes, the electrochemical characterization of their clusters is essential to understand their biological function. Complementary EPR studies were performed.
Fil: Grazina, Raquel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Sousa, Patrícia M. Paes de. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; Argentina
Fil: Carepo, Marta S. P.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Materia
7fe Ferredoxins
Desulfovibrio Bacteria
Ironsulfur Clusters
Electrochemistry
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/15146
Acceder
id CONICETDig_c63135364d6a9faa21b067b1ce4f5d63
oai_identifier_str oai:ri.conicet.gov.ar:11336/15146
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensisGrazina, RaquelSousa, Patrícia M. Paes deBrondino, Carlos DanteCarepo, Marta S. P.Moura, IsabelMoura, José J. G.7fe FerredoxinsDesulfovibrio BacteriaIronsulfur ClustersElectrochemistryhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The redox behaviour of a ferredoxin (Fd) from Desulfovibrio alaskensis was characterized by electrochemistry. The protein was isolated and purified, and showed to be a tetramer containing one [3Fe–4S] and one [4Fe–4S] centre. This ferredoxin has high homology with FdI from Desulfovibrio vulgaris Miyazaki and Hildenborough and FdIII from Desulfovibrio africanus. From differential pulse voltammetry the following signals were identified: [3Fe-4S]+ 1/0 (E0′ = − 158 ± 5 mV); [4Fe–4S]+ 2/+1 (E0′ = − 474 ± 5 mV) and [3Fe–4S]0/− 2 (E0′ = − 660 ± 5 mV). The effect of pH on these signals showed that the reduced [3Fe–4S]0 cluster has a pKʹred′ = 5.1 ± 0.1, the [4Fe–4S]+ 2/+1 centre is pH independent, and the [3Fe–4S]0/−2 reduction is accompanied by the binding of two protons. The ability of the [3Fe–4S]0 cluster to be converted into a new [4Fe–4S] cluster was proven. The redox potential of the original [4Fe–4S] centre showed to be dependent on the formation of the new [4Fe-4S] centre, which results in a positive shift (ca. 70 mV) of the redox potential of the original centre. Being most [Fe–S] proteins involved in electron transport processes, the electrochemical characterization of their clusters is essential to understand their biological function. Complementary EPR studies were performed.Fil: Grazina, Raquel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; PortugalFil: Sousa, Patrícia M. Paes de. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; PortugalFil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; ArgentinaFil: Carepo, Marta S. P.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; PortugalFil: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; PortugalFil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; PortugalElsevier2011-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/15146Grazina, Raquel; Sousa, Patrícia M. Paes de; Brondino, Carlos Dante; Carepo, Marta S. P.; Moura, Isabel; et al.; Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis; Elsevier; Bioelectrochemistry; 82; 1; 4-2011; 22-281567-5394enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bioelechem.2011.04.005info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1567539411000454info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:50:47Zoai:ri.conicet.gov.ar:11336/15146instacron: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:34982025-09-03 09:50:48.087CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
title Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
spellingShingle Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
Grazina, Raquel
7fe Ferredoxins
Desulfovibrio Bacteria
Ironsulfur Clusters
Electrochemistry
title_short Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
title_full Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
title_fullStr Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
title_full_unstemmed Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
title_sort Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis
dc.creator.none.fl_str_mv Grazina, Raquel
Sousa, Patrícia M. Paes de
Brondino, Carlos Dante
Carepo, Marta S. P.
Moura, Isabel
Moura, José J. G.
author Grazina, Raquel
author_facet Grazina, Raquel
Sousa, Patrícia M. Paes de
Brondino, Carlos Dante
Carepo, Marta S. P.
Moura, Isabel
Moura, José J. G.
author_role author
author2 Sousa, Patrícia M. Paes de
Brondino, Carlos Dante
Carepo, Marta S. P.
Moura, Isabel
Moura, José J. G.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv 7fe Ferredoxins
Desulfovibrio Bacteria
Ironsulfur Clusters
Electrochemistry
topic 7fe Ferredoxins
Desulfovibrio Bacteria
Ironsulfur Clusters
Electrochemistry
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 redox behaviour of a ferredoxin (Fd) from Desulfovibrio alaskensis was characterized by electrochemistry. The protein was isolated and purified, and showed to be a tetramer containing one [3Fe–4S] and one [4Fe–4S] centre. This ferredoxin has high homology with FdI from Desulfovibrio vulgaris Miyazaki and Hildenborough and FdIII from Desulfovibrio africanus. From differential pulse voltammetry the following signals were identified: [3Fe-4S]+ 1/0 (E0′ = − 158 ± 5 mV); [4Fe–4S]+ 2/+1 (E0′ = − 474 ± 5 mV) and [3Fe–4S]0/− 2 (E0′ = − 660 ± 5 mV). The effect of pH on these signals showed that the reduced [3Fe–4S]0 cluster has a pKʹred′ = 5.1 ± 0.1, the [4Fe–4S]+ 2/+1 centre is pH independent, and the [3Fe–4S]0/−2 reduction is accompanied by the binding of two protons. The ability of the [3Fe–4S]0 cluster to be converted into a new [4Fe–4S] cluster was proven. The redox potential of the original [4Fe–4S] centre showed to be dependent on the formation of the new [4Fe-4S] centre, which results in a positive shift (ca. 70 mV) of the redox potential of the original centre. Being most [Fe–S] proteins involved in electron transport processes, the electrochemical characterization of their clusters is essential to understand their biological function. Complementary EPR studies were performed.
Fil: Grazina, Raquel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Sousa, Patrícia M. Paes de. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; Argentina
Fil: Carepo, Marta S. P.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
Fil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Química. REQUIMTE/CQFB; Portugal
description The redox behaviour of a ferredoxin (Fd) from Desulfovibrio alaskensis was characterized by electrochemistry. The protein was isolated and purified, and showed to be a tetramer containing one [3Fe–4S] and one [4Fe–4S] centre. This ferredoxin has high homology with FdI from Desulfovibrio vulgaris Miyazaki and Hildenborough and FdIII from Desulfovibrio africanus. From differential pulse voltammetry the following signals were identified: [3Fe-4S]+ 1/0 (E0′ = − 158 ± 5 mV); [4Fe–4S]+ 2/+1 (E0′ = − 474 ± 5 mV) and [3Fe–4S]0/− 2 (E0′ = − 660 ± 5 mV). The effect of pH on these signals showed that the reduced [3Fe–4S]0 cluster has a pKʹred′ = 5.1 ± 0.1, the [4Fe–4S]+ 2/+1 centre is pH independent, and the [3Fe–4S]0/−2 reduction is accompanied by the binding of two protons. The ability of the [3Fe–4S]0 cluster to be converted into a new [4Fe–4S] cluster was proven. The redox potential of the original [4Fe–4S] centre showed to be dependent on the formation of the new [4Fe-4S] centre, which results in a positive shift (ca. 70 mV) of the redox potential of the original centre. Being most [Fe–S] proteins involved in electron transport processes, the electrochemical characterization of their clusters is essential to understand their biological function. Complementary EPR studies were performed.
publishDate 2011
dc.date.none.fl_str_mv 2011-04
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/11336/15146
Grazina, Raquel; Sousa, Patrícia M. Paes de; Brondino, Carlos Dante; Carepo, Marta S. P.; Moura, Isabel; et al.; Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis; Elsevier; Bioelectrochemistry; 82; 1; 4-2011; 22-28
1567-5394
url http://hdl.handle.net/11336/15146
identifier_str_mv Grazina, Raquel; Sousa, Patrícia M. Paes de; Brondino, Carlos Dante; Carepo, Marta S. P.; Moura, Isabel; et al.; Structural redox control in a 7Fe ferredoxin isolated from Desulfovibrio alaskensis; Elsevier; Bioelectrochemistry; 82; 1; 4-2011; 22-28
1567-5394
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bioelechem.2011.04.005
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1567539411000454
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.13397

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