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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/153465
Ver los metadatos del registro completo
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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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1844613398089695232 |
score |
13.070432 |