Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role

Autores
González, Pablo Javier; Rivas, Maria Gabriela; Mota, Cristiano S.; Brondino, Carlos Dante; Moura, Isabel; Moura, José J.G.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mo- and W-enzymes are widely distributed in biology as they can be found in all domains of life. They perform key roles in several metabolic pathways catalyzing important reactions of the biogeochemical cycles of the more abundant elements of the earth. These reactions are usually redox processes involving the transfer of an atom from the substrate to the metal ion or vice versa. The Mo or W reactivity and specificity toward a substrate is determined by the polypeptide chain of the enzyme, which tunes the chemical properties of the metal ion. Two enzymes sharing almost identical active sites but catalyzing very different reactions are periplasmic nitrate reductase and formate dehydrogenase from bacteria. They represent a good example of how key changes in the amino acid sequence tune the properties of an enzyme. In order to analyze the chemistry of Mo and W in these enzymes, structural, kinetic and spectroscopic data are reviewed, along with the role of these enzymes in cell metabolism. In addition, the features that govern selectivity of metal uptake into the cell and Mo/W-cofactor biosynthesis are revised.
Fil: González, Pablo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Rivas, Maria Gabriela. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Mota, Cristiano S.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Brondino, Carlos Dante. 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: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Moura, José J.G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Materia
Molybdenum
Tungsten
Nitrate Reductase
Formate Dehydrogenase
Catalytic Mechanism
Metal Selectivity
Moco/Wco Biosynthesis
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:11336/18986
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/18986
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic roleGonzález, Pablo JavierRivas, Maria GabrielaMota, Cristiano S.Brondino, Carlos DanteMoura, IsabelMoura, José J.G.MolybdenumTungstenNitrate ReductaseFormate DehydrogenaseCatalytic MechanismMetal SelectivityMoco/Wco Biosynthesishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Mo- and W-enzymes are widely distributed in biology as they can be found in all domains of life. They perform key roles in several metabolic pathways catalyzing important reactions of the biogeochemical cycles of the more abundant elements of the earth. These reactions are usually redox processes involving the transfer of an atom from the substrate to the metal ion or vice versa. The Mo or W reactivity and specificity toward a substrate is determined by the polypeptide chain of the enzyme, which tunes the chemical properties of the metal ion. Two enzymes sharing almost identical active sites but catalyzing very different reactions are periplasmic nitrate reductase and formate dehydrogenase from bacteria. They represent a good example of how key changes in the amino acid sequence tune the properties of an enzyme. In order to analyze the chemistry of Mo and W in these enzymes, structural, kinetic and spectroscopic data are reviewed, along with the role of these enzymes in cell metabolism. In addition, the features that govern selectivity of metal uptake into the cell and Mo/W-cofactor biosynthesis are revised.Fil: González, Pablo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; PortugalFil: Rivas, Maria Gabriela. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Mota, Cristiano S.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; PortugalFil: Brondino, Carlos Dante. 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: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; PortugalFil: Moura, José J.G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; PortugalElsevier2013-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18986González, Pablo Javier; Rivas, Maria Gabriela; Mota, Cristiano S.; Brondino, Carlos Dante; Moura, Isabel; et al.; Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role; Elsevier; Coordination Chemistry Reviews; 257; 2; 1-2013; 315-3310010-8545CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1016/j.ccr.2012.05.020info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0010854512001348?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:09Zoai:ri.conicet.gov.ar:11336/18986instacron: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 09:49:09.587CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
title Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
spellingShingle Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
González, Pablo Javier
Molybdenum
Tungsten
Nitrate Reductase
Formate Dehydrogenase
Catalytic Mechanism
Metal Selectivity
Moco/Wco Biosynthesis
title_short Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
title_full Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
title_fullStr Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
title_full_unstemmed Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
title_sort Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role
dc.creator.none.fl_str_mv González, Pablo Javier
Rivas, Maria Gabriela
Mota, Cristiano S.
Brondino, Carlos Dante
Moura, Isabel
Moura, José J.G.
author González, Pablo Javier
author_facet González, Pablo Javier
Rivas, Maria Gabriela
Mota, Cristiano S.
Brondino, Carlos Dante
Moura, Isabel
Moura, José J.G.
author_role author
author2 Rivas, Maria Gabriela
Mota, Cristiano S.
Brondino, Carlos Dante
Moura, Isabel
Moura, José J.G.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Molybdenum
Tungsten
Nitrate Reductase
Formate Dehydrogenase
Catalytic Mechanism
Metal Selectivity
Moco/Wco Biosynthesis
topic Molybdenum
Tungsten
Nitrate Reductase
Formate Dehydrogenase
Catalytic Mechanism
Metal Selectivity
Moco/Wco Biosynthesis
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Mo- and W-enzymes are widely distributed in biology as they can be found in all domains of life. They perform key roles in several metabolic pathways catalyzing important reactions of the biogeochemical cycles of the more abundant elements of the earth. These reactions are usually redox processes involving the transfer of an atom from the substrate to the metal ion or vice versa. The Mo or W reactivity and specificity toward a substrate is determined by the polypeptide chain of the enzyme, which tunes the chemical properties of the metal ion. Two enzymes sharing almost identical active sites but catalyzing very different reactions are periplasmic nitrate reductase and formate dehydrogenase from bacteria. They represent a good example of how key changes in the amino acid sequence tune the properties of an enzyme. In order to analyze the chemistry of Mo and W in these enzymes, structural, kinetic and spectroscopic data are reviewed, along with the role of these enzymes in cell metabolism. In addition, the features that govern selectivity of metal uptake into the cell and Mo/W-cofactor biosynthesis are revised.
Fil: González, Pablo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Rivas, Maria Gabriela. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Mota, Cristiano S.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Brondino, Carlos Dante. 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: Moura, Isabel. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
Fil: Moura, José J.G.. Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia. Departamento de Quimica; Portugal
description Mo- and W-enzymes are widely distributed in biology as they can be found in all domains of life. They perform key roles in several metabolic pathways catalyzing important reactions of the biogeochemical cycles of the more abundant elements of the earth. These reactions are usually redox processes involving the transfer of an atom from the substrate to the metal ion or vice versa. The Mo or W reactivity and specificity toward a substrate is determined by the polypeptide chain of the enzyme, which tunes the chemical properties of the metal ion. Two enzymes sharing almost identical active sites but catalyzing very different reactions are periplasmic nitrate reductase and formate dehydrogenase from bacteria. They represent a good example of how key changes in the amino acid sequence tune the properties of an enzyme. In order to analyze the chemistry of Mo and W in these enzymes, structural, kinetic and spectroscopic data are reviewed, along with the role of these enzymes in cell metabolism. In addition, the features that govern selectivity of metal uptake into the cell and Mo/W-cofactor biosynthesis are revised.
publishDate 2013
dc.date.none.fl_str_mv 2013-01
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/11336/18986
González, Pablo Javier; Rivas, Maria Gabriela; Mota, Cristiano S.; Brondino, Carlos Dante; Moura, Isabel; et al.; Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role; Elsevier; Coordination Chemistry Reviews; 257; 2; 1-2013; 315-331
0010-8545
CONICET Digital
CONICET
url http://hdl.handle.net/11336/18986
identifier_str_mv González, Pablo Javier; Rivas, Maria Gabriela; Mota, Cristiano S.; Brondino, Carlos Dante; Moura, Isabel; et al.; Periplasmic nitrate reductases and formate dehydrogenases: control of the chemical properties of Mo and W for fine tuning of reactivity and substrate specificity and metabolic role; Elsevier; Coordination Chemistry Reviews; 257; 2; 1-2013; 315-331
0010-8545
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://dx.doi.org/10.1016/j.ccr.2012.05.020
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0010854512001348?via%3Dihub
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
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
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score 12.885934

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