Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonocl...

Autores
Marangon, Jacopo; Paes De Sousa, Patrícia M.; Moura, Isabel; Brondino, Carlos Dante; Moura, José J. G.; González, Pablo J.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The respiratory nitrate reductase complex (NarGHI) from Marinobacter hydrocarbonoclasticus 617 (Mh, formerly Pseudomonas nautica 617) catalyzes the reduction of nitrate to nitrite. This reaction is the first step of the denitrification pathway and is coupled to the quinone pool oxidation and proton translocation to the periplasm, which generates the proton motive force needed for ATP synthesis. The Mh NarGH water-soluble heterodimer has been purified and the kinetic and redox properties have been studied through in-solution enzyme kinetics, protein film voltammetry and spectropotentiometric redox titration. The kinetic parameters of Mh NarGH toward substrates and inhibitors are consistent with those reported for other respiratory nitrate reductases. Protein film voltammetry showed that at least two catalytically distinct forms of the enzyme, which depend on the applied potential, are responsible for substrate reduction. These two forms are affected differentially by the oxidizing substrate, as well as by pH and inhibitors. A new model for the potential dependence of the catalytic efficiency of Nars is proposed.
Fil: Marangon, Jacopo. Universidade Nova de Lisboa; Portugal
Fil: Paes De Sousa, Patrícia M.. Universidade Nova de Lisboa; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa; 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, José J. G.. Universidade Nova de Lisboa; Portugal
Fil: González, Pablo J.. Universidade Nova de Lisboa; Portugal
Materia
DENITRIFICATION
ENZYME CATALYSIS
MOLYBDENUM
NITRATE REDUCTASE
PROTEIN FILM VOLTAMMETRY
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:11336/197167
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/197167
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617Marangon, JacopoPaes De Sousa, Patrícia M.Moura, IsabelBrondino, Carlos DanteMoura, José J. G.González, Pablo J.DENITRIFICATIONENZYME CATALYSISMOLYBDENUMNITRATE REDUCTASEPROTEIN FILM VOLTAMMETRYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The respiratory nitrate reductase complex (NarGHI) from Marinobacter hydrocarbonoclasticus 617 (Mh, formerly Pseudomonas nautica 617) catalyzes the reduction of nitrate to nitrite. This reaction is the first step of the denitrification pathway and is coupled to the quinone pool oxidation and proton translocation to the periplasm, which generates the proton motive force needed for ATP synthesis. The Mh NarGH water-soluble heterodimer has been purified and the kinetic and redox properties have been studied through in-solution enzyme kinetics, protein film voltammetry and spectropotentiometric redox titration. The kinetic parameters of Mh NarGH toward substrates and inhibitors are consistent with those reported for other respiratory nitrate reductases. Protein film voltammetry showed that at least two catalytically distinct forms of the enzyme, which depend on the applied potential, are responsible for substrate reduction. These two forms are affected differentially by the oxidizing substrate, as well as by pH and inhibitors. A new model for the potential dependence of the catalytic efficiency of Nars is proposed.Fil: Marangon, Jacopo. Universidade Nova de Lisboa; PortugalFil: Paes De Sousa, Patrícia M.. Universidade Nova de Lisboa; PortugalFil: Moura, Isabel. Universidade Nova de Lisboa; 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, José J. G.. Universidade Nova de Lisboa; PortugalFil: González, Pablo J.. Universidade Nova de Lisboa; PortugalElsevier Science2012-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/197167Marangon, Jacopo; Paes De Sousa, Patrícia M.; Moura, Isabel; Brondino, Carlos Dante; Moura, José J. G.; et al.; Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1817; 7; 7-2012; 1072-10820005-2728CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005272812001338info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbabio.2012.04.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:07:28Zoai:ri.conicet.gov.ar:11336/197167instacron: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:34982025-10-22 12:07:29.12CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
title Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
spellingShingle Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
Marangon, Jacopo
DENITRIFICATION
ENZYME CATALYSIS
MOLYBDENUM
NITRATE REDUCTASE
PROTEIN FILM VOLTAMMETRY
title_short Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
title_full Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
title_fullStr Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
title_full_unstemmed Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
title_sort Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
dc.creator.none.fl_str_mv Marangon, Jacopo
Paes De Sousa, Patrícia M.
Moura, Isabel
Brondino, Carlos Dante
Moura, José J. G.
González, Pablo J.
author Marangon, Jacopo
author_facet Marangon, Jacopo
Paes De Sousa, Patrícia M.
Moura, Isabel
Brondino, Carlos Dante
Moura, José J. G.
González, Pablo J.
author_role author
author2 Paes De Sousa, Patrícia M.
Moura, Isabel
Brondino, Carlos Dante
Moura, José J. G.
González, Pablo J.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv DENITRIFICATION
ENZYME CATALYSIS
MOLYBDENUM
NITRATE REDUCTASE
PROTEIN FILM VOLTAMMETRY
topic DENITRIFICATION
ENZYME CATALYSIS
MOLYBDENUM
NITRATE REDUCTASE
PROTEIN FILM VOLTAMMETRY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The respiratory nitrate reductase complex (NarGHI) from Marinobacter hydrocarbonoclasticus 617 (Mh, formerly Pseudomonas nautica 617) catalyzes the reduction of nitrate to nitrite. This reaction is the first step of the denitrification pathway and is coupled to the quinone pool oxidation and proton translocation to the periplasm, which generates the proton motive force needed for ATP synthesis. The Mh NarGH water-soluble heterodimer has been purified and the kinetic and redox properties have been studied through in-solution enzyme kinetics, protein film voltammetry and spectropotentiometric redox titration. The kinetic parameters of Mh NarGH toward substrates and inhibitors are consistent with those reported for other respiratory nitrate reductases. Protein film voltammetry showed that at least two catalytically distinct forms of the enzyme, which depend on the applied potential, are responsible for substrate reduction. These two forms are affected differentially by the oxidizing substrate, as well as by pH and inhibitors. A new model for the potential dependence of the catalytic efficiency of Nars is proposed.
Fil: Marangon, Jacopo. Universidade Nova de Lisboa; Portugal
Fil: Paes De Sousa, Patrícia M.. Universidade Nova de Lisboa; Portugal
Fil: Moura, Isabel. Universidade Nova de Lisboa; 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, José J. G.. Universidade Nova de Lisboa; Portugal
Fil: González, Pablo J.. Universidade Nova de Lisboa; Portugal
description The respiratory nitrate reductase complex (NarGHI) from Marinobacter hydrocarbonoclasticus 617 (Mh, formerly Pseudomonas nautica 617) catalyzes the reduction of nitrate to nitrite. This reaction is the first step of the denitrification pathway and is coupled to the quinone pool oxidation and proton translocation to the periplasm, which generates the proton motive force needed for ATP synthesis. The Mh NarGH water-soluble heterodimer has been purified and the kinetic and redox properties have been studied through in-solution enzyme kinetics, protein film voltammetry and spectropotentiometric redox titration. The kinetic parameters of Mh NarGH toward substrates and inhibitors are consistent with those reported for other respiratory nitrate reductases. Protein film voltammetry showed that at least two catalytically distinct forms of the enzyme, which depend on the applied potential, are responsible for substrate reduction. These two forms are affected differentially by the oxidizing substrate, as well as by pH and inhibitors. A new model for the potential dependence of the catalytic efficiency of Nars is proposed.
publishDate 2012
dc.date.none.fl_str_mv 2012-07
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/11336/197167
Marangon, Jacopo; Paes De Sousa, Patrícia M.; Moura, Isabel; Brondino, Carlos Dante; Moura, José J. G.; et al.; Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1817; 7; 7-2012; 1072-1082
0005-2728
CONICET Digital
CONICET
url http://hdl.handle.net/11336/197167
identifier_str_mv Marangon, Jacopo; Paes De Sousa, Patrícia M.; Moura, Isabel; Brondino, Carlos Dante; Moura, José J. G.; et al.; Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1817; 7; 7-2012; 1072-1082
0005-2728
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/article/pii/S0005272812001338
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbabio.2012.04.011
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
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1846782439352958976
score 12.982451

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