Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreduct...

Autores
González, Pablo Javier; Rivas, Maria Gabriela; Pérez, Ana Laura; Brondino, Carlos Dante
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature. The metal ions are either present as mononuclear centers or are organized in clusters. One of the metal cofactors is the active site of the enzyme where the substrate is converted to a product, while the others serve as electron transfer centers. Metal cofactors are paramagnetic in certain protein redox states and may additionally exhibit different relaxation rates and weak superexchange interactions transferred via intraprotein electron transfer pathways. Cu-containing nitrite reductase and Mo-containing aldehyde oxidoreductase are two representative examples of oxidoreductases in which these phenomena occur, making them interesting systems to study using electron magnetic resonance techniques. We summarize here several X-band Continuous-Wave Electron Paramagnetic Resonance (CW-EPR) studies that have allowed insights into structural and functional aspects of these two proteins and may help characterize closely related systems.
Fil: González, Pablo Javier. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Pérez, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Brondino, Carlos Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Materia
DIPOLAR INTERACTION
EPR SPECTROSCOPY
EXCHANGE INTERACTION
OXIDOREDUCTASE
REDOX ENZYME
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/224776
Acceder
id CONICETDig_7778347d99a19612968b2d3a6b53985c
oai_identifier_str oai:ri.conicet.gov.ar:11336/224776
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductaseGonzález, Pablo JavierRivas, Maria GabrielaPérez, Ana LauraBrondino, Carlos DanteDIPOLAR INTERACTIONEPR SPECTROSCOPYEXCHANGE INTERACTIONOXIDOREDUCTASEREDOX ENZYMEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature. The metal ions are either present as mononuclear centers or are organized in clusters. One of the metal cofactors is the active site of the enzyme where the substrate is converted to a product, while the others serve as electron transfer centers. Metal cofactors are paramagnetic in certain protein redox states and may additionally exhibit different relaxation rates and weak superexchange interactions transferred via intraprotein electron transfer pathways. Cu-containing nitrite reductase and Mo-containing aldehyde oxidoreductase are two representative examples of oxidoreductases in which these phenomena occur, making them interesting systems to study using electron magnetic resonance techniques. We summarize here several X-band Continuous-Wave Electron Paramagnetic Resonance (CW-EPR) studies that have allowed insights into structural and functional aspects of these two proteins and may help characterize closely related systems.Fil: González, Pablo Javier. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Pérez, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaFil: Brondino, Carlos Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaElsevier2023-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/224776González, Pablo Javier; Rivas, Maria Gabriela; Pérez, Ana Laura; Brondino, Carlos Dante; Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase; Elsevier; Journal of Magnetic Resonance Open; 16-17; 4-2023; 1-112666-4410CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S2666441023000250info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmro.2023.100117info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:41:38Zoai:ri.conicet.gov.ar:11336/224776instacron: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 09:41:38.985CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
title Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
spellingShingle Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
González, Pablo Javier
DIPOLAR INTERACTION
EPR SPECTROSCOPY
EXCHANGE INTERACTION
OXIDOREDUCTASE
REDOX ENZYME
title_short Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
title_full Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
title_fullStr Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
title_full_unstemmed Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
title_sort Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase
dc.creator.none.fl_str_mv González, Pablo Javier
Rivas, Maria Gabriela
Pérez, Ana Laura
Brondino, Carlos Dante
author González, Pablo Javier
author_facet González, Pablo Javier
Rivas, Maria Gabriela
Pérez, Ana Laura
Brondino, Carlos Dante
author_role author
author2 Rivas, Maria Gabriela
Pérez, Ana Laura
Brondino, Carlos Dante
author2_role author
author
author
dc.subject.none.fl_str_mv DIPOLAR INTERACTION
EPR SPECTROSCOPY
EXCHANGE INTERACTION
OXIDOREDUCTASE
REDOX ENZYME
topic DIPOLAR INTERACTION
EPR SPECTROSCOPY
EXCHANGE INTERACTION
OXIDOREDUCTASE
REDOX ENZYME
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature. The metal ions are either present as mononuclear centers or are organized in clusters. One of the metal cofactors is the active site of the enzyme where the substrate is converted to a product, while the others serve as electron transfer centers. Metal cofactors are paramagnetic in certain protein redox states and may additionally exhibit different relaxation rates and weak superexchange interactions transferred via intraprotein electron transfer pathways. Cu-containing nitrite reductase and Mo-containing aldehyde oxidoreductase are two representative examples of oxidoreductases in which these phenomena occur, making them interesting systems to study using electron magnetic resonance techniques. We summarize here several X-band Continuous-Wave Electron Paramagnetic Resonance (CW-EPR) studies that have allowed insights into structural and functional aspects of these two proteins and may help characterize closely related systems.
Fil: González, Pablo Javier. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Pérez, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Brondino, Carlos Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
description Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature. The metal ions are either present as mononuclear centers or are organized in clusters. One of the metal cofactors is the active site of the enzyme where the substrate is converted to a product, while the others serve as electron transfer centers. Metal cofactors are paramagnetic in certain protein redox states and may additionally exhibit different relaxation rates and weak superexchange interactions transferred via intraprotein electron transfer pathways. Cu-containing nitrite reductase and Mo-containing aldehyde oxidoreductase are two representative examples of oxidoreductases in which these phenomena occur, making them interesting systems to study using electron magnetic resonance techniques. We summarize here several X-band Continuous-Wave Electron Paramagnetic Resonance (CW-EPR) studies that have allowed insights into structural and functional aspects of these two proteins and may help characterize closely related systems.
publishDate 2023
dc.date.none.fl_str_mv 2023-04
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/11336/224776
González, Pablo Javier; Rivas, Maria Gabriela; Pérez, Ana Laura; Brondino, Carlos Dante; Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase; Elsevier; Journal of Magnetic Resonance Open; 16-17; 4-2023; 1-11
2666-4410
CONICET Digital
CONICET
url http://hdl.handle.net/11336/224776
identifier_str_mv González, Pablo Javier; Rivas, Maria Gabriela; Pérez, Ana Laura; Brondino, Carlos Dante; Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase; Elsevier; Journal of Magnetic Resonance Open; 16-17; 4-2023; 1-11
2666-4410
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://linkinghub.elsevier.com/retrieve/pii/S2666441023000250
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmro.2023.100117
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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_ 1844613313879605248
score 13.070432

Publicaciones similares