Glutathione Complexed Fe–S Centers
- Autores
- Qi, Wenbin; Li, Jingwei; Chain, Cecilia Yamil; Pasquevich, Gustavo Alberto; Pasquevich, A. F.; Cowan, J. A.
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.
Fil: Qi, Wenbin. Ohio State University; Estados Unidos
Fil: Li, Jingwei. Ohio State University; Estados Unidos
Fil: Chain, Cecilia Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; Argentina
Fil: Pasquevich, Gustavo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; Argentina
Fil: Pasquevich, A. F.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Física; Argentina
Fil: Cowan, J. A.. Ohio State University; Estados Unidos - Materia
-
GLUTATHIONE
IRON SULFUR CLUSTER
ISU
BIOGENESIS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/268550
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Glutathione Complexed Fe–S CentersQi, WenbinLi, JingweiChain, Cecilia YamilPasquevich, Gustavo AlbertoPasquevich, A. F.Cowan, J. A.GLUTATHIONEIRON SULFUR CLUSTERISUBIOGENESIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.Fil: Qi, Wenbin. Ohio State University; Estados UnidosFil: Li, Jingwei. Ohio State University; Estados UnidosFil: Chain, Cecilia Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; ArgentinaFil: Pasquevich, Gustavo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; ArgentinaFil: Pasquevich, A. F.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Física; ArgentinaFil: Cowan, J. A.. Ohio State University; Estados UnidosAmerican Chemical Society2012-06info: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/11336/268550Qi, Wenbin; Li, Jingwei; Chain, Cecilia Yamil; Pasquevich, Gustavo Alberto; Pasquevich, A. F.; et al.; Glutathione Complexed Fe–S Centers; American Chemical Society; Journal of the American Chemical Society; 134; 26; 6-2012; 10745-107480002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ja302186jinfo:eu-repo/semantics/altIdentifier/doi/10.1021/ja302186jinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:07:12Zoai:ri.conicet.gov.ar:11336/268550instacron: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:34982025-10-15 15:07:12.991CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Glutathione Complexed Fe–S Centers |
title |
Glutathione Complexed Fe–S Centers |
spellingShingle |
Glutathione Complexed Fe–S Centers Qi, Wenbin GLUTATHIONE IRON SULFUR CLUSTER ISU BIOGENESIS |
title_short |
Glutathione Complexed Fe–S Centers |
title_full |
Glutathione Complexed Fe–S Centers |
title_fullStr |
Glutathione Complexed Fe–S Centers |
title_full_unstemmed |
Glutathione Complexed Fe–S Centers |
title_sort |
Glutathione Complexed Fe–S Centers |
dc.creator.none.fl_str_mv |
Qi, Wenbin Li, Jingwei Chain, Cecilia Yamil Pasquevich, Gustavo Alberto Pasquevich, A. F. Cowan, J. A. |
author |
Qi, Wenbin |
author_facet |
Qi, Wenbin Li, Jingwei Chain, Cecilia Yamil Pasquevich, Gustavo Alberto Pasquevich, A. F. Cowan, J. A. |
author_role |
author |
author2 |
Li, Jingwei Chain, Cecilia Yamil Pasquevich, Gustavo Alberto Pasquevich, A. F. Cowan, J. A. |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
GLUTATHIONE IRON SULFUR CLUSTER ISU BIOGENESIS |
topic |
GLUTATHIONE IRON SULFUR CLUSTER ISU BIOGENESIS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione. Fil: Qi, Wenbin. Ohio State University; Estados Unidos Fil: Li, Jingwei. Ohio State University; Estados Unidos Fil: Chain, Cecilia Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; Argentina Fil: Pasquevich, Gustavo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física La Plata. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física La Plata; Argentina Fil: Pasquevich, A. F.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Física; Argentina Fil: Cowan, J. A.. Ohio State University; Estados Unidos |
description |
Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione.γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM.1 Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe2S2] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe2S2] cluster under physiological conditions, with optical, redox, Mössbauer and NMR characteristics that are consistent with a [Fe2S2](GS)4 composition. The Fe-S assembly protein ISU catalyzes formation of [Fe2S2](GS)4 from iron and sulfide ions in the presence of glutathione, and the [Fe2S2] core undergoes reversible exchange between apo ISU and free glutathione. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-06 |
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/11336/268550 Qi, Wenbin; Li, Jingwei; Chain, Cecilia Yamil; Pasquevich, Gustavo Alberto; Pasquevich, A. F.; et al.; Glutathione Complexed Fe–S Centers; American Chemical Society; Journal of the American Chemical Society; 134; 26; 6-2012; 10745-10748 0002-7863 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/268550 |
identifier_str_mv |
Qi, Wenbin; Li, Jingwei; Chain, Cecilia Yamil; Pasquevich, Gustavo Alberto; Pasquevich, A. F.; et al.; Glutathione Complexed Fe–S Centers; American Chemical Society; Journal of the American Chemical Society; 134; 26; 6-2012; 10745-10748 0002-7863 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ja302186j info:eu-repo/semantics/altIdentifier/doi/10.1021/ja302186j |
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 |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.22299 |