EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagne...

Autores
González, Pablo J.; Barrera, Guillermo Ignacio; Rizzi, Alberto Claudio; Moura, José J.G.; Passeggi, Mario Cesar Genaro; Brondino, Carlos Dante
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Electron transfer proteins and redox enzymes containing paramagnetic redox centers with different relaxation rates are widespread in nature. Despite both the long distances and chemical paths connecting these centers, they can present weak magnetic couplings produced by spin-spin interactions such as dipolar and isotropic exchange. We present here a theoretical model based on the Bloch-Wangsness-Redfield theory to analyze the dependence with temperature of EPR spectra of interacting pairs of spin 1/2 centers having different relaxation rates, as is the case of the molybdenum-containing enzyme aldehyde oxidoreductase from Desulfovibrio gigas. We analyze the changes of the EPR spectra of the slow relaxing center (Mo(V)) induced by the faster relaxing center (FeS center). At high temperatures, when the relaxation time T(1) of the fast relaxing center is very short, the magnetic coupling between centers is averaged to zero. Conversely, at low temperatures when T(1) is longer, no modulation of the coupling between metal centers can be detected.
Fil: González, Pablo J.. Universidade Nova de Lisboa; Portugal
Fil: Barrera, Guillermo Ignacio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Moura, José J.G.. Universidade Nova de Lisboa; Portugal
Fil: Passeggi, Mario Cesar Genaro. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Brondino, Carlos Dante. Universidade Nova de Lisboa; Portugal
Materia
Electron paramagnetic resonance
Magnetic interactions
Relaxation rate
Molybdenum-containing enzymes
Aldehyde oxidoreductase
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:11336/103970
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/103970
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation ratesGonzález, Pablo J.Barrera, Guillermo IgnacioRizzi, Alberto ClaudioMoura, José J.G.Passeggi, Mario Cesar GenaroBrondino, Carlos DanteElectron paramagnetic resonanceMagnetic interactionsRelaxation rateMolybdenum-containing enzymesAldehyde oxidoreductasehttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1Electron transfer proteins and redox enzymes containing paramagnetic redox centers with different relaxation rates are widespread in nature. Despite both the long distances and chemical paths connecting these centers, they can present weak magnetic couplings produced by spin-spin interactions such as dipolar and isotropic exchange. We present here a theoretical model based on the Bloch-Wangsness-Redfield theory to analyze the dependence with temperature of EPR spectra of interacting pairs of spin 1/2 centers having different relaxation rates, as is the case of the molybdenum-containing enzyme aldehyde oxidoreductase from Desulfovibrio gigas. We analyze the changes of the EPR spectra of the slow relaxing center (Mo(V)) induced by the faster relaxing center (FeS center). At high temperatures, when the relaxation time T(1) of the fast relaxing center is very short, the magnetic coupling between centers is averaged to zero. Conversely, at low temperatures when T(1) is longer, no modulation of the coupling between metal centers can be detected.Fil: González, Pablo J.. Universidade Nova de Lisboa; PortugalFil: Barrera, Guillermo Ignacio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaFil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaFil: Moura, José J.G.. Universidade Nova de Lisboa; PortugalFil: Passeggi, Mario Cesar Genaro. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; ArgentinaFil: Brondino, Carlos Dante. Universidade Nova de Lisboa; PortugalElsevier Science Inc2009-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/103970González, Pablo J.; Barrera, Guillermo Ignacio; Rizzi, Alberto Claudio; Moura, José J.G.; Passeggi, Mario Cesar Genaro; et al.; EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates; Elsevier Science Inc; Journal of Inorganic Biochemistry; 103; 10; 10-2009; 1342-13460162-0134CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGG-4WMDHDS-1&_user=10&_coverDate=10%2F31%2F2009&_rdoc=1&_fmt=high&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=ce3f8025970029951f634c8a69d5bce9info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2009.06.006info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:54:23Zoai:ri.conicet.gov.ar:11336/103970instacron: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 09:54:24.002CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
title EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
spellingShingle EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
González, Pablo J.
Electron paramagnetic resonance
Magnetic interactions
Relaxation rate
Molybdenum-containing enzymes
Aldehyde oxidoreductase
title_short EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
title_full EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
title_fullStr EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
title_full_unstemmed EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
title_sort EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates
dc.creator.none.fl_str_mv González, Pablo J.
Barrera, Guillermo Ignacio
Rizzi, Alberto Claudio
Moura, José J.G.
Passeggi, Mario Cesar Genaro
Brondino, Carlos Dante
author González, Pablo J.
author_facet González, Pablo J.
Barrera, Guillermo Ignacio
Rizzi, Alberto Claudio
Moura, José J.G.
Passeggi, Mario Cesar Genaro
Brondino, Carlos Dante
author_role author
author2 Barrera, Guillermo Ignacio
Rizzi, Alberto Claudio
Moura, José J.G.
Passeggi, Mario Cesar Genaro
Brondino, Carlos Dante
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Electron paramagnetic resonance
Magnetic interactions
Relaxation rate
Molybdenum-containing enzymes
Aldehyde oxidoreductase
topic Electron paramagnetic resonance
Magnetic interactions
Relaxation rate
Molybdenum-containing enzymes
Aldehyde oxidoreductase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Electron transfer proteins and redox enzymes containing paramagnetic redox centers with different relaxation rates are widespread in nature. Despite both the long distances and chemical paths connecting these centers, they can present weak magnetic couplings produced by spin-spin interactions such as dipolar and isotropic exchange. We present here a theoretical model based on the Bloch-Wangsness-Redfield theory to analyze the dependence with temperature of EPR spectra of interacting pairs of spin 1/2 centers having different relaxation rates, as is the case of the molybdenum-containing enzyme aldehyde oxidoreductase from Desulfovibrio gigas. We analyze the changes of the EPR spectra of the slow relaxing center (Mo(V)) induced by the faster relaxing center (FeS center). At high temperatures, when the relaxation time T(1) of the fast relaxing center is very short, the magnetic coupling between centers is averaged to zero. Conversely, at low temperatures when T(1) is longer, no modulation of the coupling between metal centers can be detected.
Fil: González, Pablo J.. Universidade Nova de Lisboa; Portugal
Fil: Barrera, Guillermo Ignacio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Rizzi, Alberto Claudio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Moura, José J.G.. Universidade Nova de Lisboa; Portugal
Fil: Passeggi, Mario Cesar Genaro. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
Fil: Brondino, Carlos Dante. Universidade Nova de Lisboa; Portugal
description Electron transfer proteins and redox enzymes containing paramagnetic redox centers with different relaxation rates are widespread in nature. Despite both the long distances and chemical paths connecting these centers, they can present weak magnetic couplings produced by spin-spin interactions such as dipolar and isotropic exchange. We present here a theoretical model based on the Bloch-Wangsness-Redfield theory to analyze the dependence with temperature of EPR spectra of interacting pairs of spin 1/2 centers having different relaxation rates, as is the case of the molybdenum-containing enzyme aldehyde oxidoreductase from Desulfovibrio gigas. We analyze the changes of the EPR spectra of the slow relaxing center (Mo(V)) induced by the faster relaxing center (FeS center). At high temperatures, when the relaxation time T(1) of the fast relaxing center is very short, the magnetic coupling between centers is averaged to zero. Conversely, at low temperatures when T(1) is longer, no modulation of the coupling between metal centers can be detected.
publishDate 2009
dc.date.none.fl_str_mv 2009-10
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/11336/103970
González, Pablo J.; Barrera, Guillermo Ignacio; Rizzi, Alberto Claudio; Moura, José J.G.; Passeggi, Mario Cesar Genaro; et al.; EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates; Elsevier Science Inc; Journal of Inorganic Biochemistry; 103; 10; 10-2009; 1342-1346
0162-0134
CONICET Digital
CONICET
url http://hdl.handle.net/11336/103970
identifier_str_mv González, Pablo J.; Barrera, Guillermo Ignacio; Rizzi, Alberto Claudio; Moura, José J.G.; Passeggi, Mario Cesar Genaro; et al.; EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch–Wangsness–Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates; Elsevier Science Inc; Journal of Inorganic Biochemistry; 103; 10; 10-2009; 1342-1346
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/http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGG-4WMDHDS-1&_user=10&_coverDate=10%2F31%2F2009&_rdoc=1&_fmt=high&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=ce3f8025970029951f634c8a69d5bce9
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2009.06.006
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
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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