PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase

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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,...

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Autor principal: Reyes, A.M
Otros Autores: Vazquez, D.S, Zeida, A., Hugo, M., Piñeyro, M.D, De Armas, M.I, Estrin, D., Radi, R., Santos, J., Trujillo, M.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Elsevier Inc. 2016
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-84994291367 
024 7 |2 cas  |a deoxycholate sodium, 302-95-4; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; thioredoxin, 52500-60-4; aldehyde dehydrogenase, 37353-37-0, 9028-86-8; hydrogen peroxide, 7722-84-1; peroxiredoxin, 207137-51-7; Aldehyde Oxidoreductases; Bacterial Proteins; fatty acid reductase; Fatty Acids; Hydrogen Peroxide; Peroxiredoxins; Recombinant Proteins; Thioredoxins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a FRBME 
100 1 |a Reyes, A.M. 
245 1 0 |a PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase 
260 |b Elsevier Inc.  |c 2016 
270 1 0 |m Trujillo, M.; Departamento de Bioquímica, Facultad de Medicina, Universidad de la RepúblicaUruguay; email: madiat@fmed.edu.uy 
506 |2 openaire  |e Política editorial 
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520 3 |a 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. © 2016 Elsevier Inc.  |l eng 
536 |a Detalles de la financiación: Universidad de la República Uruguay 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Secretaría de Ciencia y Técnica, Universidad de Buenos Aires, 20020130100097BA, 20020130100468BA 
536 |a Detalles de la financiación: 767 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT2013-0982, PICT2014-1022 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, PIP-11220110100723 
536 |a Detalles de la financiación: This work was supported by grants from Universidad de la República (CSIC Grupos 767 and Espacio Interdisciplinario), CONICET ( PIP-11220110100723 ), ANPCyT ( PICT2014-1022 and PICT2013-0982 ) and UBACyT ( 20020130100097BA and 20020130100468BA ). A. M. Reyes was partially supported by a PhD scholarship from Universidad de la República-CAP, Uruguay and D.S. Vazquez was supported by a PhD scholarship from Universidad de Buenos Aires , Argentina. 
593 |a Departamento de Bioquímica, Facultad de Medicina, Universidad de la RepúblicaMontevideo, Uruguay 
593 |a Center for Free Radical and Biomedical Research, Universidad de la RepúblicaMontevideo, Uruguay 
593 |a Instituto de Química y Físicoquímica Biológicas “Prof. Alejandro C. Paladini” (IQUIFIB), Universidad de Buenos Aires and CONICET, Ciudad Autónoma de Buenos Aires, Argentina 
593 |a Departamento de Química Inorgánica, Analítica y Química-Física, INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a Unidad de Biología Molecular-Institut Pasteur MontevideoMontevideo, Uruguay 
690 1 0 |a FATTY ACID HYDROPEROXIDES 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a PEROXIDATIC AND RESOLVING CYSTEINE 
690 1 0 |a PEROXIREDOXIN 
690 1 0 |a PEROXYNITRITE 
690 1 0 |a THIOL-DEPENDENT PEROXIDASE 
690 1 0 |a THIOREDOXIN 
690 1 0 |a DEOXYCHOLATE SODIUM 
690 1 0 |a OXIDOREDUCTASE 
690 1 0 |a PEROXIREDOXIN Q B 
690 1 0 |a PEROXYNITRITE 
690 1 0 |a REDUCING AGENT 
690 1 0 |a THIOREDOXIN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ALDEHYDE DEHYDROGENASE 
690 1 0 |a BACTERIAL PROTEIN 
690 1 0 |a FATTY ACID 
690 1 0 |a FATTY ACID REDUCTASE 
690 1 0 |a HYDROGEN PEROXIDE 
690 1 0 |a PEROXIREDOXIN 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a RECOMBINANT PROTEIN 
690 1 0 |a THIOREDOXIN 
690 1 0 |a ARTICLE 
690 1 0 |a BACTERIAL GROWTH 
690 1 0 |a CATALYSIS 
690 1 0 |a CIRCULAR DICHROISM 
690 1 0 |a CONFORMATIONAL TRANSITION 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME CONFORMATION 
690 1 0 |a HYDRODYNAMICS 
690 1 0 |a HYDROGEN BOND 
690 1 0 |a HYDROPHOBICITY 
690 1 0 |a MOLECULAR DYNAMICS 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a NONHUMAN 
690 1 0 |a OBSERVED RATE CONSTANT 
690 1 0 |a OXIDATION 
690 1 0 |a OXIDATION REDUCTION STATE 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN SECONDARY STRUCTURE 
690 1 0 |a PROTEIN STRUCTURE 
690 1 0 |a PROTEIN TERTIARY STRUCTURE 
690 1 0 |a REDUCTION 
690 1 0 |a SEQUENCE HOMOLOGY 
690 1 0 |a STEADY STATE 
690 1 0 |a ALPHA HELIX 
690 1 0 |a BETA SHEET 
690 1 0 |a BINDING SITE 
690 1 0 |a CHEMISTRY 
690 1 0 |a ENZYME SPECIFICITY 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a GENE VECTOR 
690 1 0 |a GENETICS 
690 1 0 |a KINETICS 
690 1 0 |a METABOLISM 
690 1 0 |a MOLECULAR CLONING 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a OXIDATION REDUCTION REACTION 
690 1 0 |a PROTEIN DOMAIN 
690 1 0 |a PROTEIN MOTIF 
690 1 0 |a ALDEHYDE OXIDOREDUCTASES 
690 1 0 |a AMINO ACID MOTIFS 
690 1 0 |a BACTERIAL PROTEINS 
690 1 0 |a BINDING SITES 
690 1 0 |a CLONING, MOLECULAR 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a FATTY ACIDS 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a GENETIC VECTORS 
690 1 0 |a HYDROGEN PEROXIDE 
690 1 0 |a KINETICS 
690 1 0 |a MOLECULAR DYNAMICS SIMULATION 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a OXIDATION-REDUCTION 
690 1 0 |a PEROXIREDOXINS 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN CONFORMATION, ALPHA-HELICAL 
690 1 0 |a PROTEIN CONFORMATION, BETA-STRAND 
690 1 0 |a PROTEIN INTERACTION DOMAINS AND MOTIFS 
690 1 0 |a RECOMBINANT PROTEINS 
690 1 0 |a SUBSTRATE SPECIFICITY 
690 1 0 |a THIOREDOXINS 
700 1 |a Vazquez, D.S. 
700 1 |a Zeida, A. 
700 1 |a Hugo, M. 
700 1 |a Piñeyro, M.D. 
700 1 |a De Armas, M.I. 
700 1 |a Estrin, D. 
700 1 |a Radi, R. 
700 1 |a Santos, J. 
700 1 |a Trujillo, M. 
773 0 |d Elsevier Inc., 2016  |g v. 101  |h pp. 249-260  |p Free Radic. Biol. Med.  |x 08915849  |w (AR-BaUEN)CENRE-4784  |t Free Radical Biology and Medicine 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-84994291367&doi=10.1016%2fj.freeradbiomed.2016.10.005&partnerID=40&md5=aa272e86bbb4da4d712f9fdb22260205  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1016/j.freeradbiomed.2016.10.005  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_08915849_v101_n_p249_Reyes  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08915849_v101_n_p249_Reyes  |y Registro en la Biblioteca Digital 
961 |a paper_08915849_v101_n_p249_Reyes  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 76477 

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