Studying Electron Transfer Pathways in Oxidoreductases

Autores
Rivas, Maria Gabriela; González, Pablo Javier; Ferroni, Felix Martín; Rizzi, Alberto Claudio; Brondino, Carlos Dante
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.
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: 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: Ferroni, Felix Martín. 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: Rizzi, Alberto Claudio. 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
electron transfer pathways
oxidoreductases
transition metal ions
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:11336/174603
Acceder
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spelling Studying Electron Transfer Pathways in OxidoreductasesRivas, Maria GabrielaGonzález, Pablo JavierFerroni, Felix MartínRizzi, Alberto ClaudioBrondino, Carlos Danteelectron transfer pathwaysoxidoreductasestransition metal ionshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.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; ArgentinaFil: 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: Ferroni, Felix Martín. 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: Rizzi, Alberto Claudio. 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; ArgentinaCentro de Estudios sobre Ciencia, Desarrollo y Educación Superior2020-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/174603Rivas, Maria Gabriela; González, Pablo Javier; Ferroni, Felix Martín; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Studying Electron Transfer Pathways in Oxidoreductases; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews; 1; 2; 3-2020; 6-232683-9288CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.scirevfew.net/index.php/sciencereviews/article/view/15info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:09:18Zoai:ri.conicet.gov.ar:11336/174603instacron: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 10:09:18.618CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Studying Electron Transfer Pathways in Oxidoreductases
title Studying Electron Transfer Pathways in Oxidoreductases
spellingShingle Studying Electron Transfer Pathways in Oxidoreductases
Rivas, Maria Gabriela
electron transfer pathways
oxidoreductases
transition metal ions
title_short Studying Electron Transfer Pathways in Oxidoreductases
title_full Studying Electron Transfer Pathways in Oxidoreductases
title_fullStr Studying Electron Transfer Pathways in Oxidoreductases
title_full_unstemmed Studying Electron Transfer Pathways in Oxidoreductases
title_sort Studying Electron Transfer Pathways in Oxidoreductases
dc.creator.none.fl_str_mv Rivas, Maria Gabriela
González, Pablo Javier
Ferroni, Felix Martín
Rizzi, Alberto Claudio
Brondino, Carlos Dante
author Rivas, Maria Gabriela
author_facet Rivas, Maria Gabriela
González, Pablo Javier
Ferroni, Felix Martín
Rizzi, Alberto Claudio
Brondino, Carlos Dante
author_role author
author2 González, Pablo Javier
Ferroni, Felix Martín
Rizzi, Alberto Claudio
Brondino, Carlos Dante
author2_role author
author
author
author
dc.subject.none.fl_str_mv electron transfer pathways
oxidoreductases
transition metal ions
topic electron transfer pathways
oxidoreductases
transition metal ions
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.
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: 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: Ferroni, Felix Martín. 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: Rizzi, Alberto Claudio. 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 Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.
publishDate 2020
dc.date.none.fl_str_mv 2020-03
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/11336/174603
Rivas, Maria Gabriela; González, Pablo Javier; Ferroni, Felix Martín; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Studying Electron Transfer Pathways in Oxidoreductases; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews; 1; 2; 3-2020; 6-23
2683-9288
CONICET Digital
CONICET
url http://hdl.handle.net/11336/174603
identifier_str_mv Rivas, Maria Gabriela; González, Pablo Javier; Ferroni, Felix Martín; Rizzi, Alberto Claudio; Brondino, Carlos Dante; Studying Electron Transfer Pathways in Oxidoreductases; Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior; Science Reviews; 1; 2; 3-2020; 6-23
2683-9288
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.scirevfew.net/index.php/sciencereviews/article/view/15
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 Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior
publisher.none.fl_str_mv Centro de Estudios sobre Ciencia, Desarrollo y Educación Superior
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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