NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p

Autores
Zaballa, María Eugenia; Ziegler, Lynn; Kosman, Daniel J.; Vila, Alejandro Jose
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe2+to Fe3+. The electronic structure of the different copper centers in this family of enzymes has beenextensively studied and discussed for years with a particular focus on the exchange coupling regimein the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu2+ ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.
Fil: Zaballa, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Ziegler, Lynn. University of New York; Estados Unidos
Fil: Kosman, Daniel J.. University of New York; Estados Unidos
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
Ceruloplasmin/chemistry
Ceruloplasmin/metabolism
Copper
Electron Spin Resonance Spectroscopy
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:11336/278574
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3pZaballa, María EugeniaZiegler, LynnKosman, Daniel J.Vila, Alejandro JoseCeruloplasmin/chemistryCeruloplasmin/metabolismCopperElectron Spin Resonance Spectroscopyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe2+to Fe3+. The electronic structure of the different copper centers in this family of enzymes has beenextensively studied and discussed for years with a particular focus on the exchange coupling regimein the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu2+ ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.Fil: Zaballa, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Ziegler, Lynn. University of New York; Estados UnidosFil: Kosman, Daniel J.. University of New York; Estados UnidosFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaAmerican Chemical Society2010-07info: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/11336/278574Zaballa, María Eugenia; Ziegler, Lynn; Kosman, Daniel J.; Vila, Alejandro Jose; NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p; American Chemical Society; Journal of the American Chemical Society; 132; 32; 7-2010; 11191-111960002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/full/10.1021/ja1037148info:eu-repo/semantics/altIdentifier/doi/10.1021/ja1037148info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-11T13:25:38Zoai:ri.conicet.gov.ar:11336/278574instacron: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:34982026-02-11 13:25:39.037CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
title NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
spellingShingle NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
Zaballa, María Eugenia
Ceruloplasmin/chemistry
Ceruloplasmin/metabolism
Copper
Electron Spin Resonance Spectroscopy
title_short NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
title_full NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
title_fullStr NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
title_full_unstemmed NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
title_sort NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
dc.creator.none.fl_str_mv Zaballa, María Eugenia
Ziegler, Lynn
Kosman, Daniel J.
Vila, Alejandro Jose
author Zaballa, María Eugenia
author_facet Zaballa, María Eugenia
Ziegler, Lynn
Kosman, Daniel J.
Vila, Alejandro Jose
author_role author
author2 Ziegler, Lynn
Kosman, Daniel J.
Vila, Alejandro Jose
author2_role author
author
author
dc.subject.none.fl_str_mv Ceruloplasmin/chemistry
Ceruloplasmin/metabolism
Copper
Electron Spin Resonance Spectroscopy
topic Ceruloplasmin/chemistry
Ceruloplasmin/metabolism
Copper
Electron Spin Resonance Spectroscopy
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe2+to Fe3+. The electronic structure of the different copper centers in this family of enzymes has beenextensively studied and discussed for years with a particular focus on the exchange coupling regimein the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu2+ ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.
Fil: Zaballa, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Ziegler, Lynn. University of New York; Estados Unidos
Fil: Kosman, Daniel J.. University of New York; Estados Unidos
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe2+to Fe3+. The electronic structure of the different copper centers in this family of enzymes has beenextensively studied and discussed for years with a particular focus on the exchange coupling regimein the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu2+ ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.
publishDate 2010
dc.date.none.fl_str_mv 2010-07
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/11336/278574
Zaballa, María Eugenia; Ziegler, Lynn; Kosman, Daniel J.; Vila, Alejandro Jose; NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p; American Chemical Society; Journal of the American Chemical Society; 132; 32; 7-2010; 11191-11196
0002-7863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/278574
identifier_str_mv Zaballa, María Eugenia; Ziegler, Lynn; Kosman, Daniel J.; Vila, Alejandro Jose; NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p; American Chemical Society; Journal of the American Chemical Society; 132; 32; 7-2010; 11191-11196
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/full/10.1021/ja1037148
info:eu-repo/semantics/altIdentifier/doi/10.1021/ja1037148
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
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 12.930639

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