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dc.contributor.author
Reyes, Aníbal M
dc.contributor.author
Hugo. Martín
dc.contributor.author
Trostchansky, Andrés
dc.contributor.author
Capece, Luciana
dc.contributor.author
Radi, Rafael
dc.contributor.author
Trujillo, Madia
dc.date.available
2017-05-03T19:58:49Z
dc.date.issued
2011-07
dc.identifier.citation
Reyes, Aníbal M; Hugo. Martín; Trostchansky, Andrés; Capece, Luciana; Radi, Rafael; et al.; Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation; Elsevier Inc; Free Radical Biology And Medicine; 51; 2; 7-2011; 464-473
dc.identifier.issn
0891-5849
dc.identifier.uri
http://hdl.handle.net/11336/15936
dc.description.abstract
Alkyl hydroperoxide reductase E (AhpE), a novel subgroup of the peroxiredoxin family, comprises Mycobacterium tuberculosis AhpE (MtAhpE) and AhpE-like proteins present in many bacteria and archaea, for which functional characterization is scarce. We previously reported that MtAhpE reacted ~ 103 times faster with peroxynitrite than with hydrogen peroxide, but the molecular reasons for that remained unknown. Herein, we investigated the oxidizing substrate specificity and the oxidative inactivation of the enzyme. In most cases, both peroxidatic thiol oxidation and sulfenic acid overoxidation followed a trend in which those peroxides with the lower leaving-group pKa reacted faster than others. These data are in agreement with the accepted mechanisms of thiol oxidation and support that overoxidation occurs through sulfenate anion reaction with the protonated peroxide. However, MtAhpE oxidation and overoxidation by fatty acid-derived hydroperoxides (~ 108 and 105 M− 1 s− 1, respectively, at pH 7.4 and 25 °C) were much faster than expected according to the Brønsted relationship with leaving-group pKa. A stoichiometric reduction of the arachidonic acid hydroperoxide 15-HpETE to its corresponding alcohol was confirmed. Interactions of fatty acid hydroperoxides with a hydrophobic groove present on the reduced MtAhpE surface could be the basis of their surprisingly fast reactivity.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Mycobacterium Tuberculosis
dc.subject
Peroxiredoxin
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Alkyl Hydroperoxide Reductase E
dc.subject
Free Radicals
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-05-02T20:59:21Z
dc.journal.volume
51
dc.journal.number
2
dc.journal.pagination
464-473
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: Hugo. Martín. Universidad de la República; Uruguay
dc.description.fil
Fil: Trostchansky, Andrés. Universidad de la República; Uruguay
dc.description.fil
Fil: Capece, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de Los Materiales, Medioambiente y Energia; Argentina
dc.description.fil
Fil: Radi, Rafael. Universidad de la República; Uruguay
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/http://dx.doi.org/10.1016/j.freeradbiomed.2011.04.023
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0891584911002498
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