Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins

Autores
Lancaster, Kyle M.; Zaballa, María Eugenia; Sproules, Stephen; Sundararajan, Mahesh; DeBeer, Serena; Richards, John H.; Vila, Alejandro Jose; Neese, Frank; Gray, Harry B.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called "type zero" sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.
Fil: Lancaster, Kyle M.. California Institute of Technology; Estados Unidos. Cornell University; Estados Unidos
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: Sproules, Stephen. University of Manchester; Reino Unido
Fil: Sundararajan, Mahesh. Universitat Bonn; Alemania
Fil: DeBeer, Serena. Cornell University; Estados Unidos
Fil: Richards, John H.. California Institute of Technology; 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: Neese, Frank. Universitat Bonn; Alemania
Fil: Gray, Harry B.. California Institute of Technology; Estados Unidos
Materia
electron transfer
copper proteins
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:11336/268426
Acceder
id CONICETDig_a718fc10eb8369af246eaab5019e24ae
oai_identifier_str oai:ri.conicet.gov.ar:11336/268426
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper ProteinsLancaster, Kyle M.Zaballa, María EugeniaSproules, StephenSundararajan, MaheshDeBeer, SerenaRichards, John H.Vila, Alejandro JoseNeese, FrankGray, Harry B.electron transfercopper proteinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called "type zero" sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.Fil: Lancaster, Kyle M.. California Institute of Technology; Estados Unidos. Cornell University; Estados UnidosFil: 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: Sproules, Stephen. University of Manchester; Reino UnidoFil: Sundararajan, Mahesh. Universitat Bonn; AlemaniaFil: DeBeer, Serena. Cornell University; Estados UnidosFil: Richards, John H.. California Institute of Technology; 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: Neese, Frank. Universitat Bonn; AlemaniaFil: Gray, Harry B.. California Institute of Technology; Estados UnidosAmerican Chemical Society2012-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/268426Lancaster, Kyle M.; Zaballa, María Eugenia; Sproules, Stephen; Sundararajan, Mahesh; DeBeer, Serena; et al.; Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins; American Chemical Society; Journal of the American Chemical Society; 134; 19; 5-2012; 8241-82530002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/ja302190rinfo:eu-repo/semantics/altIdentifier/doi/10.1021/ja302190rinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:32:30Zoai:ri.conicet.gov.ar:11336/268426instacron: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 09:32:31.216CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
title Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
spellingShingle Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
Lancaster, Kyle M.
electron transfer
copper proteins
title_short Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
title_full Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
title_fullStr Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
title_full_unstemmed Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
title_sort Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins
dc.creator.none.fl_str_mv Lancaster, Kyle M.
Zaballa, María Eugenia
Sproules, Stephen
Sundararajan, Mahesh
DeBeer, Serena
Richards, John H.
Vila, Alejandro Jose
Neese, Frank
Gray, Harry B.
author Lancaster, Kyle M.
author_facet Lancaster, Kyle M.
Zaballa, María Eugenia
Sproules, Stephen
Sundararajan, Mahesh
DeBeer, Serena
Richards, John H.
Vila, Alejandro Jose
Neese, Frank
Gray, Harry B.
author_role author
author2 Zaballa, María Eugenia
Sproules, Stephen
Sundararajan, Mahesh
DeBeer, Serena
Richards, John H.
Vila, Alejandro Jose
Neese, Frank
Gray, Harry B.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv electron transfer
copper proteins
topic electron transfer
copper proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called "type zero" sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.
Fil: Lancaster, Kyle M.. California Institute of Technology; Estados Unidos. Cornell University; Estados Unidos
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: Sproules, Stephen. University of Manchester; Reino Unido
Fil: Sundararajan, Mahesh. Universitat Bonn; Alemania
Fil: DeBeer, Serena. Cornell University; Estados Unidos
Fil: Richards, John H.. California Institute of Technology; 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: Neese, Frank. Universitat Bonn; Alemania
Fil: Gray, Harry B.. California Institute of Technology; Estados Unidos
description Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called "type zero" sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.
publishDate 2012
dc.date.none.fl_str_mv 2012-05
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/11336/268426
Lancaster, Kyle M.; Zaballa, María Eugenia; Sproules, Stephen; Sundararajan, Mahesh; DeBeer, Serena; et al.; Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins; American Chemical Society; Journal of the American Chemical Society; 134; 19; 5-2012; 8241-8253
0002-7863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/268426
identifier_str_mv Lancaster, Kyle M.; Zaballa, María Eugenia; Sproules, Stephen; Sundararajan, Mahesh; DeBeer, Serena; et al.; Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins; American Chemical Society; Journal of the American Chemical Society; 134; 19; 5-2012; 8241-8253
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/https://pubs.acs.org/doi/10.1021/ja302190r
info:eu-repo/semantics/altIdentifier/doi/10.1021/ja302190r
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
_version_ 1844612991969918976
score 13.070432

Publicaciones similares