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Kinetic studies of peroxiredoxin 6 from Arenicola marina: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide
Loumaye, E.; Ferrer-Sueta, G.; Alvarez, B.; Rees, J.-F.; Clippe, A.; Knoops, B.; Radi, R.; Trujillo, M. (2011). Kinetic studies of peroxiredoxin 6 from Arenicola marina: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide. Arch. Biochem. Biophys. 514(1-2): 1-7. http://dx.doi.org/10.1016/j.abb.2011.07.002
In: Archives of biochemistry and biophysics. ELSEVIER SCIENCE INC: San Diego, CA,. ISSN 0003-9861; e-ISSN 1096-0384, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoord
    Marien/Kust
Author keywords
    Peroxiredoxins; Oxidative stress; Kinetics; Hydrogen peroxide; Peroxynitrite; Hydrogen sulfide
Auteurs  Top 
  • Loumaye, E., meer
  • Ferrer-Sueta, G.
  • Alvarez, B.
  • Rees, J.-F., meer
  • Clippe, A., meer
  • Knoops, B., meer
  • Radi, R.
  • Trujillo, M.
Abstract
    Arenicola marina lives in marine environments where hydrogen peroxide concentrations reach micromolar levels. The annelid also forms reactive species through metabolic pathways. Its antioxidant systems include a cytosolic peroxiredoxin, peroxiredoxin 6 (AmPrx6 or AmPRDX6) that shows high homology to the mammalian 1-Cys peroxiredoxin. Previous work confirmed the peroxidase activity of AmPrx6 in the presence of dithiotreitol. Herein, we performed an in vitro kinetic characterization of the recombinant enzyme. AmPrx6 reduced hydrogen peroxide and peroxynitrite with rate constants of 1.1 × 107 and 2 × 106 M-1 s-1, respectively, at pH 7.4 and 25 °C. Reduction of tert-butyl hydroperoxide was slower. The pKa of the peroxidatic thiol of AmPrx6 was determined as 5.1 ± 0.2, indicating that it exists as thiolate, the reactive species, at physiological pH. The reductive part of the catalytic cycle was also explored. Hydrogen sulfide, present in millimolar concentrations in marine sediments where the annelid lives and that is able to reduce the mammalian 1-Cys peroxiredoxin, did not support AmPrx6 peroxidase activity. The enzyme was not reduced by other potential physiological reductants tested. Our data indicate that in this annelid, Prx6 could contribute to peroxide detoxification in the presence of a so far unidentified reducing counterpart.
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