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dc.contributor.author
Marangon, Jacopo
dc.contributor.author
Paes De Sousa, Patrícia M.
dc.contributor.author
Moura, Isabel
dc.contributor.author
Brondino, Carlos Dante
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dc.contributor.author
Moura, José J. G.
dc.contributor.author
González, Pablo J.
dc.date.available
2023-05-11T13:20:10Z
dc.date.issued
2012-07
dc.identifier.citation
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
dc.identifier.issn
0005-2728
dc.identifier.uri
http://hdl.handle.net/11336/197167
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
DENITRIFICATION
dc.subject
ENZYME CATALYSIS
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MOLYBDENUM
dc.subject
NITRATE REDUCTASE
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PROTEIN FILM VOLTAMMETRY
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-04-28T10:46:03Z
dc.journal.volume
1817
dc.journal.number
7
dc.journal.pagination
1072-1082
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Marangon, Jacopo. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Paes De Sousa, Patrícia M.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Moura, Isabel. Universidade Nova de Lisboa; Portugal
dc.description.fil
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
dc.description.fil
Fil: Moura, José J. G.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: González, Pablo J.. Universidade Nova de Lisboa; Portugal
dc.journal.title
Biochimica Et Biophysica Acta-bioenergetics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005272812001338
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbabio.2012.04.011
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