Copper-substituted forms of the wild type and C42A variant of rubredoxin

Autores
Thapper, Anders; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Wedd, Anthony G.; Pais, Ricardo J.; Maiti, Biplab K.; Moura, Isabel; Pauletta,Sofia R.; Moura, José J. G.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In order to gain insights into the interplay between Cu(I) and Cu(II) in sulfur-rich protein environments, the first preparation and characterization of copper-substituted forms of the wild-type rubredoxin (Rd) from Desulfovibrio vulgaris Hildenborough are reported, as well as those of its variant C42A-Rd. The initial products appear to be tetrahedral CuI(S–Cys)n species for the wild type (n = 4) and the variant C42A (n = 3, with an additional unidentified ligand). These species are unstable to aerial oxidation to products, whose properties are consistent with square planar CuII(S–Cys)n species. These Cu(II) intermediates are susceptible to auto-reduction by ligand S–Cys to produce stable Cu(I) final products. The original Cu(I) center in the wild-type system can be regenerated by reduction, suggesting that the active site can accommodate CuI(S–Cys)2 and Cys–S–S–Cys fragments in the final product. The absence of one S–Cys ligand prevents similar regeneration in the C42A–Rd system. These results emphasize the redox instability of CuII–(S–Cys)n centers.
Fil: Thapper, Anders. Uppsala Universitet; Suecia
Fil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe; Argentina
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Wedd, Anthony G.. University of Melbourne; Australia
Fil: Pais, Ricardo J.. Universidade Nova de Lisboa; Portugal
Fil: Maiti, Biplab K.. Universidade Nova de Lisboa; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa; Portugal
Fil: Pauletta,Sofia R.. Universidade Nova de Lisboa; Portugal
Fil: Moura, José J. G.. Universidade Nova de Lisboa; Portugal
Materia
Rubredoxin
Mutant Coordination Site
Copper-Substituted Iron-Sulfur Center
Uv-Visible
Epr
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:11336/1962
Acceder
id CONICETDig_693ec400417d52604a34de97d37771fd
oai_identifier_str oai:ri.conicet.gov.ar:11336/1962
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Copper-substituted forms of the wild type and C42A variant of rubredoxinThapper, AndersRizzi, Alberto ClaudioBrondino, Carlos DanteWedd, Anthony G.Pais, Ricardo J.Maiti, Biplab K.Moura, IsabelPauletta,Sofia R.Moura, José J. G.RubredoxinMutant Coordination SiteCopper-Substituted Iron-Sulfur CenterUv-VisibleEprhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1In order to gain insights into the interplay between Cu(I) and Cu(II) in sulfur-rich protein environments, the first preparation and characterization of copper-substituted forms of the wild-type rubredoxin (Rd) from Desulfovibrio vulgaris Hildenborough are reported, as well as those of its variant C42A-Rd. The initial products appear to be tetrahedral CuI(S–Cys)n species for the wild type (n = 4) and the variant C42A (n = 3, with an additional unidentified ligand). These species are unstable to aerial oxidation to products, whose properties are consistent with square planar CuII(S–Cys)n species. These Cu(II) intermediates are susceptible to auto-reduction by ligand S–Cys to produce stable Cu(I) final products. The original Cu(I) center in the wild-type system can be regenerated by reduction, suggesting that the active site can accommodate CuI(S–Cys)2 and Cys–S–S–Cys fragments in the final product. The absence of one S–Cys ligand prevents similar regeneration in the C42A–Rd system. These results emphasize the redox instability of CuII–(S–Cys)n centers.Fil: Thapper, Anders. Uppsala Universitet; SueciaFil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe; ArgentinaFil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaFil: Wedd, Anthony G.. University of Melbourne; AustraliaFil: Pais, Ricardo J.. Universidade Nova de Lisboa; PortugalFil: Maiti, Biplab K.. Universidade Nova de Lisboa; PortugalFil: Moura, Isabel. Universidade Nova de Lisboa; PortugalFil: Pauletta,Sofia R.. Universidade Nova de Lisboa; PortugalFil: Moura, José J. G.. Universidade Nova de Lisboa; PortugalElsevier2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1962Thapper, Anders; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Wedd, Anthony G.; Pais, Ricardo J.; et al.; Copper-substituted forms of the wild type and C42A variant of rubredoxin; Elsevier; Journal of Inorganic Biochemistry; 127; 6-2013; 232-2370162-0134enginfo:eu-repo/semantics/reference/url/info:eu-repo/semantics/reference es info:eu-repo/semantics/reference/pmid/23829948info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S016201341300144Xinfo:eu-repo/semantics/altIdentifier/doi/doi:10.1016/j.jinorgbio.2013.06.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:15:01Zoai:ri.conicet.gov.ar:11336/1962instacron: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 11:15:02.231CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Copper-substituted forms of the wild type and C42A variant of rubredoxin
title Copper-substituted forms of the wild type and C42A variant of rubredoxin
spellingShingle Copper-substituted forms of the wild type and C42A variant of rubredoxin
Thapper, Anders
Rubredoxin
Mutant Coordination Site
Copper-Substituted Iron-Sulfur Center
Uv-Visible
Epr
title_short Copper-substituted forms of the wild type and C42A variant of rubredoxin
title_full Copper-substituted forms of the wild type and C42A variant of rubredoxin
title_fullStr Copper-substituted forms of the wild type and C42A variant of rubredoxin
title_full_unstemmed Copper-substituted forms of the wild type and C42A variant of rubredoxin
title_sort Copper-substituted forms of the wild type and C42A variant of rubredoxin
dc.creator.none.fl_str_mv Thapper, Anders
Rizzi, Alberto Claudio
Brondino, Carlos Dante
Wedd, Anthony G.
Pais, Ricardo J.
Maiti, Biplab K.
Moura, Isabel
Pauletta,Sofia R.
Moura, José J. G.
author Thapper, Anders
author_facet Thapper, Anders
Rizzi, Alberto Claudio
Brondino, Carlos Dante
Wedd, Anthony G.
Pais, Ricardo J.
Maiti, Biplab K.
Moura, Isabel
Pauletta,Sofia R.
Moura, José J. G.
author_role author
author2 Rizzi, Alberto Claudio
Brondino, Carlos Dante
Wedd, Anthony G.
Pais, Ricardo J.
Maiti, Biplab K.
Moura, Isabel
Pauletta,Sofia R.
Moura, José J. G.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Rubredoxin
Mutant Coordination Site
Copper-Substituted Iron-Sulfur Center
Uv-Visible
Epr
topic Rubredoxin
Mutant Coordination Site
Copper-Substituted Iron-Sulfur Center
Uv-Visible
Epr
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In order to gain insights into the interplay between Cu(I) and Cu(II) in sulfur-rich protein environments, the first preparation and characterization of copper-substituted forms of the wild-type rubredoxin (Rd) from Desulfovibrio vulgaris Hildenborough are reported, as well as those of its variant C42A-Rd. The initial products appear to be tetrahedral CuI(S–Cys)n species for the wild type (n = 4) and the variant C42A (n = 3, with an additional unidentified ligand). These species are unstable to aerial oxidation to products, whose properties are consistent with square planar CuII(S–Cys)n species. These Cu(II) intermediates are susceptible to auto-reduction by ligand S–Cys to produce stable Cu(I) final products. The original Cu(I) center in the wild-type system can be regenerated by reduction, suggesting that the active site can accommodate CuI(S–Cys)2 and Cys–S–S–Cys fragments in the final product. The absence of one S–Cys ligand prevents similar regeneration in the C42A–Rd system. These results emphasize the redox instability of CuII–(S–Cys)n centers.
Fil: Thapper, Anders. Uppsala Universitet; Suecia
Fil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe; Argentina
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Wedd, Anthony G.. University of Melbourne; Australia
Fil: Pais, Ricardo J.. Universidade Nova de Lisboa; Portugal
Fil: Maiti, Biplab K.. Universidade Nova de Lisboa; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa; Portugal
Fil: Pauletta,Sofia R.. Universidade Nova de Lisboa; Portugal
Fil: Moura, José J. G.. Universidade Nova de Lisboa; Portugal
description In order to gain insights into the interplay between Cu(I) and Cu(II) in sulfur-rich protein environments, the first preparation and characterization of copper-substituted forms of the wild-type rubredoxin (Rd) from Desulfovibrio vulgaris Hildenborough are reported, as well as those of its variant C42A-Rd. The initial products appear to be tetrahedral CuI(S–Cys)n species for the wild type (n = 4) and the variant C42A (n = 3, with an additional unidentified ligand). These species are unstable to aerial oxidation to products, whose properties are consistent with square planar CuII(S–Cys)n species. These Cu(II) intermediates are susceptible to auto-reduction by ligand S–Cys to produce stable Cu(I) final products. The original Cu(I) center in the wild-type system can be regenerated by reduction, suggesting that the active site can accommodate CuI(S–Cys)2 and Cys–S–S–Cys fragments in the final product. The absence of one S–Cys ligand prevents similar regeneration in the C42A–Rd system. These results emphasize the redox instability of CuII–(S–Cys)n centers.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/1962
Thapper, Anders; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Wedd, Anthony G.; Pais, Ricardo J.; et al.; Copper-substituted forms of the wild type and C42A variant of rubredoxin; Elsevier; Journal of Inorganic Biochemistry; 127; 6-2013; 232-237
0162-0134
url http://hdl.handle.net/11336/1962
identifier_str_mv Thapper, Anders; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Wedd, Anthony G.; Pais, Ricardo J.; et al.; Copper-substituted forms of the wild type and C42A variant of rubredoxin; Elsevier; Journal of Inorganic Biochemistry; 127; 6-2013; 232-237
0162-0134
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/reference/url/info:eu-repo/semantics/reference es info:eu-repo/semantics/reference/pmid/23829948
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S016201341300144X
info:eu-repo/semantics/altIdentifier/doi/doi:10.1016/j.jinorgbio.2013.06.003
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 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 13.234792

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