{"refrec":{"BRefID":220600,"RR":"<b>Loumaye, E.; Ferrer-Sueta, G.; Alvarez, B.; Rees, J.-F.; Clippe, A.; Knoops, B.; Radi, R.; Trujillo, M.</b> (2011). Kinetic studies of peroxiredoxin 6 from <i>Arenicola marina</i>: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide. <i>Arch. Biochem. Biophys. 514(1-2)</i>: 1-7. <a href=\"http://dx.doi.org/10.1016/j.abb.2011.07.002\" target=\"_blank\">http://dx.doi.org/10.1016/j.abb.2011.07.002</a>","BEntID":212333,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Arch. Biochem. Biophys. 514(1-2)</i>: 1-7. <a href=\"http://dx.doi.org/10.1016/j.abb.2011.07.002\" target=\"_blank\">http://dx.doi.org/10.1016/j.abb.2011.07.002</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Loumaye, E.; Ferrer-Sueta, G.; Alvarez, B.; Rees, J.-F.; Clippe, A.; Knoops, B.; Radi, R.; Trujillo, M.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Loumaye, E. <i>et al.</i>","Englishabstract":"<em>Arenicola marina</em> 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 (<em>Am</em>Prx6 or <em>Am</em>PRDX6) that shows high homology to the mammalian 1-Cys peroxiredoxin. Previous work confirmed the peroxidase activity of <em>Am</em>Prx6 in the presence of dithiotreitol. Herein, we performed an <em>in vitro</em> kinetic characterization of the recombinant enzyme. <em>Am</em>Prx6 reduced hydrogen peroxide and peroxynitrite with rate constants of 1.1 × 10<sup>7</sup> and 2 × 10<sup>6</sup> M<sup>-1</sup> s<sup>-1</sup>, respectively, at pH 7.4 and 25 °C. Reduction of <em>tert-</em>butyl hydroperoxide was slower. The p<em>K</em><sub>a</sub> of the peroxidatic thiol of <em>Am</em>Prx6 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 <em>Am</em>Prx6 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Kinetic studies of peroxiredoxin 6 from <i>Arenicola marina</i>: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-22 01:31:43.946851","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"    Peroxiredoxins;     Oxidative stress;     Kinetics;     Hydrogen peroxide;     Peroxynitrite;     Hydrogen sulfide","OtherDescriptors":null,"Notes":null,"AnaPub":2011,"MonPub":null,"DateUpdate":"2015-11-04","DateCreate":"2012-11-29","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000295190900001","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.abb.2011.07.002"},"refs":null,"anarec":{"AnaID":220600,"PubliDate":2011,"Pagination":"1-7","XtraPublOfAnaID":null,"ISBN":null,"Volume":"514","Issue":"1-2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42387,"SerRR":"Archives of biochemistry and biophysics. 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