INVESTIGADORES
IGLESIAS Alberto Alvaro
artículos
Título:
Kinetic and Structural Characterization of a Typical 2-Cysteine Peroxiredoxin from Leptospira interrogans Exhibiting Redox Sensitivity
Autor/es:
D.G. ARIAS; A. REINOSO; N. SASONI; M.D. HARTMAN; A.A. IGLESIAS; S.A. GUERRERO
Revista:
FREE RADICAL BIOLOGY AND MEDICINE
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Lugar: Amsterdam; Año: 2014 vol. 77 p. 30 - 40
ISSN:
0891-5849
Resumen:
Little isknownaboutthemechanismsbywhich Leptospirainterrogans, the causative agent ofleptospirosis,copes with oxidative stress at the time it establishes persistent infection within its human host. We report the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins). These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp 1% 30 mM at pH 7.0 and 30 1C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.
