Reyes, A.M.; Vazquez, D.S.; Zeida, A.; Hugo, M.; Piñeyro, M.D.; De Armas, M.I.; Estrin, D.; Radi, R.; Santos, J.; Trujillo, M. "PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase" (2016) Free Radical Biology and Medicine. 101:249-260
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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, 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.


Documento: Artículo
Título:PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase
Autor:Reyes, A.M.; Vazquez, D.S.; Zeida, A.; Hugo, M.; Piñeyro, M.D.; De Armas, M.I.; Estrin, D.; Radi, R.; Santos, J.; Trujillo, M.
Filiación:Departamento de Bioquímica, Facultad de Medicina, Universidad de la RepúblicaMontevideo, Uruguay
Center for Free Radical and Biomedical Research, Universidad de la RepúblicaMontevideo, Uruguay
Instituto de Química y Físicoquímica Biológicas “Prof. Alejandro C. Paladini” (IQUIFIB), Universidad de Buenos Aires and CONICET, Ciudad Autónoma de Buenos Aires, Argentina
Departamento de Química Inorgánica, Analítica y Química-Física, INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Unidad de Biología Molecular-Institut Pasteur MontevideoMontevideo, Uruguay
Palabras clave:Fatty acid hydroperoxides; Mycobacterium tuberculosis; Peroxidatic and resolving cysteine; Peroxiredoxin; Peroxynitrite; Thiol-dependent peroxidase; Thioredoxin; deoxycholate sodium; oxidoreductase; peroxiredoxin Q B; peroxynitrite; reducing agent; thioredoxin; unclassified drug; aldehyde dehydrogenase; bacterial protein; fatty acid; fatty acid reductase; hydrogen peroxide; peroxiredoxin; protein binding; recombinant protein; thioredoxin; Article; bacterial growth; catalysis; circular dichroism; conformational transition; enzyme activity; enzyme conformation; hydrodynamics; hydrogen bond; hydrophobicity; molecular dynamics; Mycobacterium tuberculosis; nonhuman; observed rate constant; oxidation; oxidation reduction state; priority journal; protein expression; protein secondary structure; protein structure; protein tertiary structure; reduction; sequence homology; steady state; alpha helix; beta sheet; binding site; chemistry; enzyme specificity; enzymology; Escherichia coli; gene expression; gene vector; genetics; kinetics; metabolism; molecular cloning; Mycobacterium tuberculosis; oxidation reduction reaction; protein domain; protein motif; Aldehyde Oxidoreductases; Amino Acid Motifs; Bacterial Proteins; Binding Sites; Cloning, Molecular; Escherichia coli; Fatty Acids; Gene Expression; Genetic Vectors; Hydrogen Peroxide; Kinetics; Molecular Dynamics Simulation; Mycobacterium tuberculosis; Oxidation-Reduction; Peroxiredoxins; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Substrate Specificity; Thioredoxins
Página de inicio:249
Página de fin:260
Título revista:Free Radical Biology and Medicine
Título revista abreviado:Free Radic. Biol. Med.
CAS: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


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---------- APA ----------
Reyes, A.M., Vazquez, D.S., Zeida, A., Hugo, M., Piñeyro, M.D., De Armas, M.I., Estrin, D.,..., Trujillo, M. (2016) . PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase. Free Radical Biology and Medicine, 101, 249-260.
---------- CHICAGO ----------
Reyes, A.M., Vazquez, D.S., Zeida, A., Hugo, M., Piñeyro, M.D., De Armas, M.I., et al. "PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase" . Free Radical Biology and Medicine 101 (2016) : 249-260.
---------- MLA ----------
Reyes, A.M., Vazquez, D.S., Zeida, A., Hugo, M., Piñeyro, M.D., De Armas, M.I., et al. "PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase" . Free Radical Biology and Medicine, vol. 101, 2016, pp. 249-260.
---------- VANCOUVER ----------
Reyes, A.M., Vazquez, D.S., Zeida, A., Hugo, M., Piñeyro, M.D., De Armas, M.I., et al. PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase. Free Radic. Biol. Med. 2016;101:249-260.