Formation and electronic structure of an atypical Cu A site

Autores
Ross, Matthew O.; Fisher, Oriana S.; Morgada, Marcos Nicolás; Krzyaniak, Matthew D.; Wasielewski, Michael R.; Vila, Alejandro Jose; Hoffman, Brian M.; Rosenzweig, Amy C.
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
PmoD, a recently discovered protein from methane-oxidizing bacteria, forms a homodimer with a dicopper CuA center at the dimer interface. Although the optical and electron paramagnetic resonance (EPR) spectroscopic signatures of the PmoD CuA bear similarities to those of canonical CuA sites, there are also some puzzling differences. Here we have characterized the rapid formation (seconds) and slow decay (hours) of this homodimeric CuA site to two mononuclear Cu2+ sites, as well as its electronic and geometric structure, using stopped-flow optical and advanced paramagnetic resonance spectroscopies. PmoD CuA formation occurs rapidly and involves a short-lived intermediate with a max of 360 nm. Unlike other CuA sites, the PmoD CuA is unstable, decaying to two type 2 Cu2+ centers. Surprisingly, NMR data indicate that the PmoD CuA has a pure σu∗ ground state rather than the typical equilibrium between σu∗ and πu of all other CuA proteins. EPR, ENDOR, ESEEM, and HYSCORE data indicate the presence of two histidine and two cysteine ligands coordinating the CuA core in a highly symmetrical fashion. This report significantly expands the diversity and understanding of known CuA sites.
Fil: Ross, Matthew O.. Northwestern University; Estados Unidos
Fil: Fisher, Oriana S.. Northwestern University; Estados Unidos
Fil: Morgada, Marcos Nicolás. 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: Krzyaniak, Matthew D.. Northwestern University; Estados Unidos
Fil: Wasielewski, Michael R.. Northwestern University; 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
Fil: Hoffman, Brian M.. Northwestern University; Estados Unidos
Fil: Rosenzweig, Amy C.. Northwestern University; Estados Unidos
Materia
CuA
PmoD
Metanotrophs
Ellectronic Structure
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:11336/153465

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network_name_str CONICET Digital (CONICET)
spelling Formation and electronic structure of an atypical Cu A siteRoss, Matthew O.Fisher, Oriana S.Morgada, Marcos NicolásKrzyaniak, Matthew D.Wasielewski, Michael R.Vila, Alejandro JoseHoffman, Brian M.Rosenzweig, Amy C.CuAPmoDMetanotrophsEllectronic Structurehttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1PmoD, a recently discovered protein from methane-oxidizing bacteria, forms a homodimer with a dicopper CuA center at the dimer interface. Although the optical and electron paramagnetic resonance (EPR) spectroscopic signatures of the PmoD CuA bear similarities to those of canonical CuA sites, there are also some puzzling differences. Here we have characterized the rapid formation (seconds) and slow decay (hours) of this homodimeric CuA site to two mononuclear Cu2+ sites, as well as its electronic and geometric structure, using stopped-flow optical and advanced paramagnetic resonance spectroscopies. PmoD CuA formation occurs rapidly and involves a short-lived intermediate with a max of 360 nm. Unlike other CuA sites, the PmoD CuA is unstable, decaying to two type 2 Cu2+ centers. Surprisingly, NMR data indicate that the PmoD CuA has a pure σu∗ ground state rather than the typical equilibrium between σu∗ and πu of all other CuA proteins. EPR, ENDOR, ESEEM, and HYSCORE data indicate the presence of two histidine and two cysteine ligands coordinating the CuA core in a highly symmetrical fashion. This report significantly expands the diversity and understanding of known CuA sites.Fil: Ross, Matthew O.. Northwestern University; Estados UnidosFil: Fisher, Oriana S.. Northwestern University; Estados UnidosFil: Morgada, Marcos Nicolás. 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: Krzyaniak, Matthew D.. Northwestern University; Estados UnidosFil: Wasielewski, Michael R.. Northwestern University; 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; ArgentinaFil: Hoffman, Brian M.. Northwestern University; Estados UnidosFil: Rosenzweig, Amy C.. Northwestern University; Estados UnidosAmerican Chemical Society2019-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/153465Ross, Matthew O.; Fisher, Oriana S.; Morgada, Marcos Nicolás; Krzyaniak, Matthew D.; Wasielewski, Michael R.; et al.; Formation and electronic structure of an atypical Cu A site; American Chemical Society; Journal of the American Chemical Society; 141; 11; 2-2019; 4678-46860002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/jacs.8b13610info:eu-repo/semantics/altIdentifier/doi/10.1021/jacs.8b13610info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:25Zoai:ri.conicet.gov.ar:11336/153465instacron: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:34982025-09-29 09:44:25.809CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Formation and electronic structure of an atypical Cu A site
title Formation and electronic structure of an atypical Cu A site
spellingShingle Formation and electronic structure of an atypical Cu A site
Ross, Matthew O.
CuA
PmoD
Metanotrophs
Ellectronic Structure
title_short Formation and electronic structure of an atypical Cu A site
title_full Formation and electronic structure of an atypical Cu A site
title_fullStr Formation and electronic structure of an atypical Cu A site
title_full_unstemmed Formation and electronic structure of an atypical Cu A site
title_sort Formation and electronic structure of an atypical Cu A site
dc.creator.none.fl_str_mv Ross, Matthew O.
Fisher, Oriana S.
Morgada, Marcos Nicolás
Krzyaniak, Matthew D.
Wasielewski, Michael R.
Vila, Alejandro Jose
Hoffman, Brian M.
Rosenzweig, Amy C.
author Ross, Matthew O.
author_facet Ross, Matthew O.
Fisher, Oriana S.
Morgada, Marcos Nicolás
Krzyaniak, Matthew D.
Wasielewski, Michael R.
Vila, Alejandro Jose
Hoffman, Brian M.
Rosenzweig, Amy C.
author_role author
author2 Fisher, Oriana S.
Morgada, Marcos Nicolás
Krzyaniak, Matthew D.
Wasielewski, Michael R.
Vila, Alejandro Jose
Hoffman, Brian M.
Rosenzweig, Amy C.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CuA
PmoD
Metanotrophs
Ellectronic Structure
topic CuA
PmoD
Metanotrophs
Ellectronic Structure
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv PmoD, a recently discovered protein from methane-oxidizing bacteria, forms a homodimer with a dicopper CuA center at the dimer interface. Although the optical and electron paramagnetic resonance (EPR) spectroscopic signatures of the PmoD CuA bear similarities to those of canonical CuA sites, there are also some puzzling differences. Here we have characterized the rapid formation (seconds) and slow decay (hours) of this homodimeric CuA site to two mononuclear Cu2+ sites, as well as its electronic and geometric structure, using stopped-flow optical and advanced paramagnetic resonance spectroscopies. PmoD CuA formation occurs rapidly and involves a short-lived intermediate with a max of 360 nm. Unlike other CuA sites, the PmoD CuA is unstable, decaying to two type 2 Cu2+ centers. Surprisingly, NMR data indicate that the PmoD CuA has a pure σu∗ ground state rather than the typical equilibrium between σu∗ and πu of all other CuA proteins. EPR, ENDOR, ESEEM, and HYSCORE data indicate the presence of two histidine and two cysteine ligands coordinating the CuA core in a highly symmetrical fashion. This report significantly expands the diversity and understanding of known CuA sites.
Fil: Ross, Matthew O.. Northwestern University; Estados Unidos
Fil: Fisher, Oriana S.. Northwestern University; Estados Unidos
Fil: Morgada, Marcos Nicolás. 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: Krzyaniak, Matthew D.. Northwestern University; Estados Unidos
Fil: Wasielewski, Michael R.. Northwestern University; 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
Fil: Hoffman, Brian M.. Northwestern University; Estados Unidos
Fil: Rosenzweig, Amy C.. Northwestern University; Estados Unidos
description PmoD, a recently discovered protein from methane-oxidizing bacteria, forms a homodimer with a dicopper CuA center at the dimer interface. Although the optical and electron paramagnetic resonance (EPR) spectroscopic signatures of the PmoD CuA bear similarities to those of canonical CuA sites, there are also some puzzling differences. Here we have characterized the rapid formation (seconds) and slow decay (hours) of this homodimeric CuA site to two mononuclear Cu2+ sites, as well as its electronic and geometric structure, using stopped-flow optical and advanced paramagnetic resonance spectroscopies. PmoD CuA formation occurs rapidly and involves a short-lived intermediate with a max of 360 nm. Unlike other CuA sites, the PmoD CuA is unstable, decaying to two type 2 Cu2+ centers. Surprisingly, NMR data indicate that the PmoD CuA has a pure σu∗ ground state rather than the typical equilibrium between σu∗ and πu of all other CuA proteins. EPR, ENDOR, ESEEM, and HYSCORE data indicate the presence of two histidine and two cysteine ligands coordinating the CuA core in a highly symmetrical fashion. This report significantly expands the diversity and understanding of known CuA sites.
publishDate 2019
dc.date.none.fl_str_mv 2019-02
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/11336/153465
Ross, Matthew O.; Fisher, Oriana S.; Morgada, Marcos Nicolás; Krzyaniak, Matthew D.; Wasielewski, Michael R.; et al.; Formation and electronic structure of an atypical Cu A site; American Chemical Society; Journal of the American Chemical Society; 141; 11; 2-2019; 4678-4686
0002-7863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/153465
identifier_str_mv Ross, Matthew O.; Fisher, Oriana S.; Morgada, Marcos Nicolás; Krzyaniak, Matthew D.; Wasielewski, Michael R.; et al.; Formation and electronic structure of an atypical Cu A site; American Chemical Society; Journal of the American Chemical Society; 141; 11; 2-2019; 4678-4686
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/10.1021/jacs.8b13610
info:eu-repo/semantics/altIdentifier/doi/10.1021/jacs.8b13610
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 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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