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dc.contributor.author
Reyes, Aníbal M.
dc.contributor.author
Vazquez, Diego Sebastian
dc.contributor.author
Zeida Camacho, Ari Fernando
dc.contributor.author
Hugo, Martín
dc.contributor.author
Piñeyro, María Dolores
dc.contributor.author
De Armas, María Inés
dc.contributor.author
Estrin, Dario Ariel
dc.contributor.author
Radi, Rafael
dc.contributor.author
Santos, Javier
dc.contributor.author
Trujillo, Madia
dc.date.available
2018-06-04T20:00:55Z
dc.date.issued
2016-12
dc.identifier.citation
Reyes, Aníbal M.; Vazquez, Diego Sebastian; Zeida Camacho, Ari Fernando; Hugo, Martín; Piñeyro, María Dolores; et al.; PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase; Elsevier Science Inc; Free Radical Biology and Medicine; 101; 12-2016; 249-260
dc.identifier.issn
0891-5849
dc.identifier.uri
http://hdl.handle.net/11336/47218
dc.description.abstract
Mycobacterium tuberculosis (M. tuberculosis) is the intracellular bacterium responsible for tuberculosis disease (TD). Inside the phagosomes of activated macrophages, M. tuberculosis is exposed to cytotoxic hydroperoxides such as hydrogen peroxide, fatty acid hydroperoxides and peroxynitrite. Thus, the characterization of the bacterial antioxidant systems could facilitate novel drug developments. In this work, we characterized the product of the gene Rv1608c from M. tuberculosis, which according to sequence homology had been annotated as a putative peroxiredoxin of the peroxiredoxin Q subfamily (PrxQ B from M. tuberculosis or MtPrxQ B). The protein has been reported to be essential for M. tuberculosis growth in cholesterol-rich medium. We demonstrated the M. tuberculosis thioredoxin B/C-dependent peroxidase activity of MtPrxQ B, which acted as a two-cysteine peroxiredoxin that could function, although less efficiently, using a one-cysteine mechanism. Through steady-state and competition kinetic analysis, we proved that the net forward rate constant of MtPrxQ B reaction was 3 orders of magnitude faster for fatty acid hydroperoxides than for hydrogen peroxide (3×106 vs 6×103 M−1 s−1, respectively), while the rate constant of peroxynitrite reduction was (0.6−1.4) ×106 M−1 s−1 at pH 7.4. The enzyme lacked activity towards cholesterol hydroperoxides solubilized in sodium deoxycholate. Both thioredoxin B and C rapidly reduced the oxidized form of MtPrxQ B, with rates constants of 0.5×106 and 1×106 M−1 s−1, respectively. Our data indicated that MtPrxQ B is monomeric in solution both under reduced and oxidized states. In spite of the similar hydrodynamic behavior the reduced and oxidized forms of the protein showed important structural differences that were reflected in the protein circular dichroism spectra.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Fatty Acid Hydroperoxides
dc.subject
Mycobacterium Tuberculosis
dc.subject
Peroxidatic And Resolving Cysteine
dc.subject
Peroxiredoxin
dc.subject
Peroxynitrite
dc.subject
Thiol-Dependent Peroxidase
dc.subject
Thioredoxin
dc.subject.classification
Otras Ciencias Biológicas
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-04T17:31:18Z
dc.journal.volume
101
dc.journal.pagination
249-260
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Reyes, Aníbal M.. Universidad de la República; Uruguay
dc.description.fil
Fil: Vazquez, Diego Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Zeida Camacho, Ari Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Hugo, Martín. Universidad de la República; Uruguay
dc.description.fil
Fil: Piñeyro, María Dolores. Universidad de la República; Uruguay. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: De Armas, María Inés. Universidad de la República; Uruguay
dc.description.fil
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Radi, Rafael. Universidad de la República; Uruguay
dc.description.fil
Fil: Santos, Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Trujillo, Madia. Universidad de la República; Uruguay
dc.journal.title
Free Radical Biology and Medicine
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.freeradbiomed.2016.10.005
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0891584916304476


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    Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"

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