X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus

Autores
Breece, Robert M.; Llarrull, Leticia Irene; Tioni, Mariana Florencia; Vila, Alejandro Jose; Tierney, David L.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cobalt and zinc binding by the subclass B1 metallo-beta-lactamase BcII from Bacillus cereus is examined by X-ray absorption spectroscopy, at various levels of metal loading. The data show that a significant amount of the dinuclear enzyme is formed, even at substoichiometric levels of metal loading, whether the added metal is Zn(II) or Co(II). Increasing metal addition, from 0.5 to 1.0 to 2.0 eq/mol of enzyme, are shown to result in a more ordered active site. While Zn(II) appears to show no preference for the Zn1 (3H) or Zn2 (DCH) sites,the extended X-ray absorption fine structure (EXAFS) suggests that Co(II) shows a slight preference for the DCH site at low levels of added Co(II). The results are discussed in the context of similar metal-binding studies of other B1 metallo-beta-lactamases.
Fil: Breece, Robert M.. Miami University; Estados Unidos
Fil: Llarrull, Leticia Irene. 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: Tioni, Mariana Florencia. 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: 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
Fil: Tierney, David L.. Miami University; Estados Unidos
Materia
EXAFS
METALLO-BETA-LACTAMASE
COBALT
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:11336/268265
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/268265
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereusBreece, Robert M.Llarrull, Leticia IreneTioni, Mariana FlorenciaVila, Alejandro JoseTierney, David L.EXAFSMETALLO-BETA-LACTAMASECOBALThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cobalt and zinc binding by the subclass B1 metallo-beta-lactamase BcII from Bacillus cereus is examined by X-ray absorption spectroscopy, at various levels of metal loading. The data show that a significant amount of the dinuclear enzyme is formed, even at substoichiometric levels of metal loading, whether the added metal is Zn(II) or Co(II). Increasing metal addition, from 0.5 to 1.0 to 2.0 eq/mol of enzyme, are shown to result in a more ordered active site. While Zn(II) appears to show no preference for the Zn1 (3H) or Zn2 (DCH) sites,the extended X-ray absorption fine structure (EXAFS) suggests that Co(II) shows a slight preference for the DCH site at low levels of added Co(II). The results are discussed in the context of similar metal-binding studies of other B1 metallo-beta-lactamases.Fil: Breece, Robert M.. Miami University; Estados UnidosFil: Llarrull, Leticia Irene. 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: Tioni, Mariana Florencia. 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: 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; ArgentinaFil: Tierney, David L.. Miami University; Estados UnidosElsevier Science Inc.2012-06info: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/11336/268265Breece, Robert M.; Llarrull, Leticia Irene; Tioni, Mariana Florencia; Vila, Alejandro Jose; Tierney, David L.; X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus; Elsevier Science Inc.; Journal of Inorganic Biochemistry; 111; 6-2012; 182-1860162-0134CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0162013412000098info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2011.12.013info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:10:24Zoai:ri.conicet.gov.ar:11336/268265instacron: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 10:10:24.863CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
title X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
spellingShingle X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
Breece, Robert M.
EXAFS
METALLO-BETA-LACTAMASE
COBALT
title_short X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
title_full X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
title_fullStr X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
title_full_unstemmed X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
title_sort X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
dc.creator.none.fl_str_mv Breece, Robert M.
Llarrull, Leticia Irene
Tioni, Mariana Florencia
Vila, Alejandro Jose
Tierney, David L.
author Breece, Robert M.
author_facet Breece, Robert M.
Llarrull, Leticia Irene
Tioni, Mariana Florencia
Vila, Alejandro Jose
Tierney, David L.
author_role author
author2 Llarrull, Leticia Irene
Tioni, Mariana Florencia
Vila, Alejandro Jose
Tierney, David L.
author2_role author
author
author
author
dc.subject.none.fl_str_mv EXAFS
METALLO-BETA-LACTAMASE
COBALT
topic EXAFS
METALLO-BETA-LACTAMASE
COBALT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cobalt and zinc binding by the subclass B1 metallo-beta-lactamase BcII from Bacillus cereus is examined by X-ray absorption spectroscopy, at various levels of metal loading. The data show that a significant amount of the dinuclear enzyme is formed, even at substoichiometric levels of metal loading, whether the added metal is Zn(II) or Co(II). Increasing metal addition, from 0.5 to 1.0 to 2.0 eq/mol of enzyme, are shown to result in a more ordered active site. While Zn(II) appears to show no preference for the Zn1 (3H) or Zn2 (DCH) sites,the extended X-ray absorption fine structure (EXAFS) suggests that Co(II) shows a slight preference for the DCH site at low levels of added Co(II). The results are discussed in the context of similar metal-binding studies of other B1 metallo-beta-lactamases.
Fil: Breece, Robert M.. Miami University; Estados Unidos
Fil: Llarrull, Leticia Irene. 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: Tioni, Mariana Florencia. 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: 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
Fil: Tierney, David L.. Miami University; Estados Unidos
description Cobalt and zinc binding by the subclass B1 metallo-beta-lactamase BcII from Bacillus cereus is examined by X-ray absorption spectroscopy, at various levels of metal loading. The data show that a significant amount of the dinuclear enzyme is formed, even at substoichiometric levels of metal loading, whether the added metal is Zn(II) or Co(II). Increasing metal addition, from 0.5 to 1.0 to 2.0 eq/mol of enzyme, are shown to result in a more ordered active site. While Zn(II) appears to show no preference for the Zn1 (3H) or Zn2 (DCH) sites,the extended X-ray absorption fine structure (EXAFS) suggests that Co(II) shows a slight preference for the DCH site at low levels of added Co(II). The results are discussed in the context of similar metal-binding studies of other B1 metallo-beta-lactamases.
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/11336/268265
Breece, Robert M.; Llarrull, Leticia Irene; Tioni, Mariana Florencia; Vila, Alejandro Jose; Tierney, David L.; X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus; Elsevier Science Inc.; Journal of Inorganic Biochemistry; 111; 6-2012; 182-186
0162-0134
CONICET Digital
CONICET
url http://hdl.handle.net/11336/268265
identifier_str_mv Breece, Robert M.; Llarrull, Leticia Irene; Tioni, Mariana Florencia; Vila, Alejandro Jose; Tierney, David L.; X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus; Elsevier Science Inc.; Journal of Inorganic Biochemistry; 111; 6-2012; 182-186
0162-0134
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0162013412000098
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2011.12.013
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 Elsevier Science Inc.
publisher.none.fl_str_mv Elsevier Science Inc.
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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