Glutathione complexed Fe-S centers

Autores
Qi, Wenbin; Li, Jingwei; Chain, Cecilia Yamil; Pasquevich, Gustavo Alberto; Pasquevich, Alberto Felipe; Cowan, James 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, Mossbauer, 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.
Facultad de Ciencias Exactas
Materia
Física
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/132235
Acceder
id SEDICI_f13b7441a890de9e1ac6af84b9a9fa3a
oai_identifier_str oai:sedici.unlp.edu.ar:10915/132235
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Glutathione complexed Fe-S centersQi, WenbinLi, JingweiChain, Cecilia YamilPasquevich, Gustavo AlbertoPasquevich, Alberto FelipeCowan, James A.FísicaGlutathione (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, Mossbauer, 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.Facultad de Ciencias Exactas2012-06-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf10745-10748http://sedici.unlp.edu.ar/handle/10915/132235enginfo:eu-repo/semantics/altIdentifier/issn/1520-5126info:eu-repo/semantics/altIdentifier/issn/0002-7863info:eu-repo/semantics/altIdentifier/doi/10.1021/ja302186jinfo:eu-repo/semantics/altIdentifier/pmid/22687047info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:23:43Zoai:sedici.unlp.edu.ar:10915/132235Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:23:43.926SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Física
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, Alberto Felipe
Cowan, James A.
author Qi, Wenbin
author_facet Qi, Wenbin
Li, Jingwei
Chain, Cecilia Yamil
Pasquevich, Gustavo Alberto
Pasquevich, Alberto Felipe
Cowan, James A.
author_role author
author2 Li, Jingwei
Chain, Cecilia Yamil
Pasquevich, Gustavo Alberto
Pasquevich, Alberto Felipe
Cowan, James A.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Física
topic Física
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, Mossbauer, 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.
Facultad de Ciencias Exactas
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, Mossbauer, 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 2012-06-21
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/132235
url http://sedici.unlp.edu.ar/handle/10915/132235
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1520-5126
info:eu-repo/semantics/altIdentifier/issn/0002-7863
info:eu-repo/semantics/altIdentifier/doi/10.1021/ja302186j
info:eu-repo/semantics/altIdentifier/pmid/22687047
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
10745-10748
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
_version_ 1846064291934896128
score 13.22299

Publicaciones similares