Reaction of low-molecular-mass organoselenium compounds (and their sulphur analogues) with inflammation-associated oxidants

References

• Gammelgaard B, Jackson MI, Gabel-Jensen C. Surveying selenium speciation from soil to cell - forms and transformations. Anal Bioanal Chem 2011;399:1743–1763.
   PubMed Web of Science ®Google Scholar
• Papp LV, Lu J, Holmgren A, Khanna KK. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antiox Redox Signal 2007;9:775–806.
   PubMed Web of Science ®Google Scholar
• Lippman SM, Goodman PJ, Klein EA, Parnes HL, Thompson IM, Kristal AR, et al.Designing the selenium and vitamin E cancer prevention trial (SELECT). J Natl Cancer Inst 2005;97:94–102.
   PubMed Web of Science ®Google Scholar
• Lippman SM, Klein EA, Goodman PJ, Lucia MS, Thompson IM, Ford LG, et al.Effect of selenium and vitamin E on risk of prostate cancer and other cancers the selenium and vitamin E cancer prevention trial (SELECT). J Am Med Assoc 2009;301:39–51.
   PubMed Web of Science ®Google Scholar
• Kristal AR, Darke AK, Morris JS, Tangen CM, Goodman PJ, Thompson IM, et al.Baseline selenium status and effects of selenium and vitamin E supplementation on prostate cancer risk. J Natl Cancer Inst 2014;106:djt456.
   Google Scholar
• Laclaustra M, Navas-Acien A, Stranges S, Ordovas JM, Guallar E. Serum selenium concentrations and diabetes in U.S. adults: National health and nutrition examination survey (NHANES) 2003-2004. Environ Health Perspect 2009;117:1409–1413.
   Web of Science ®Google Scholar
• Sieri S, Pala V, Brighenti F, Pellegrini N, Muti P, Micheli A, et al.Dietary glycemic index, glycemic load, and the risk of breast cancer in an Italian prospective cohort study. Am J Clin Nutr 2007;86:1160–1166.
   PubMed Web of Science ®Google Scholar
• Stranges S, Sieri S, Vinceti M, Grioni S, Guallar E, Laclaustra M, et al.A prospective study of dietary selenium intake and risk of type 2 diabetes. BMC Public Health 2010;10:564.
   PubMed Web of Science ®Google Scholar
• Rayman MP, Blundell-Pound G, Pastor-Barriuso R, Guallar E, Steinbrenner H, Stranges S. A randomized trial of selenium supplementation and risk of type-2 diabetes, as assessed by plasma adiponectin. PLoS One 2012;7:e45269.
   PubMed Web of Science ®Google Scholar
• Rayman MP, Stranges S. Epidemiology of selenium and type 2 diabetes: can we make sense of it? Free Radic Biol Med 2013;65:1557–1564.
   PubMed Web of Science ®Google Scholar
• Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: molecular pathways and physiological roles. Physiol Rev 2014;94:739–777.
   PubMed Web of Science ®Google Scholar
• Lu J, Holmgren A. Selenoproteins. J Biol Chem 2009;284: 723–727.
   PubMed Web of Science ®Google Scholar
• Reeves MA, Hoffmann PR. The human selenoproteome: Recent insights into functions and regulation. Cell Mol Life Sci 2009;66:2457–2478.
   PubMed Web of Science ®Google Scholar
• Murphy MP. Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications. Antiox Redox Signal 2012;16: 476–495.
   PubMed Web of Science ®Google Scholar
• Hansen RE, Roth D, Winther JR. Quantifying the global cellular thiol-disulfide status. Proc Natl Acad Sci USA 2009;106:422–427.
   PubMed Web of Science ®Google Scholar
• Requejo R, Hurd TR, Costa NJ, Murphy MP. Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage. FEBS J 2010;277:1465–1480.
   PubMed Web of Science ®Google Scholar
• Go YM, Jones DP. Thiol/disulfide redox states in signaling and sensing. Crit Rev Biochem Mol Biol 2013;48:173–181.
   PubMed Web of Science ®Google Scholar
• Turell L, Radi R, Alvarez B. The thiol pool in human plasma: the central contribution of albumin to redox processes. Free Radic Biol Med 2013;65:244–253.
   PubMed Web of Science ®Google Scholar
• Lillig CH, Holmgren A. Thioredoxin and related molecules - from biology to health and disease. Antiox Redox Signal 2007;9:25–47.
   PubMed Web of Science ®Google Scholar
• Berndt C, Lillig CH, Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 2007;292:H1227–H1236.
   PubMed Web of Science ®Google Scholar
• Rhee SG, Kang SW, Netto LE, Seo MS, Stadtman ER. A family of novel peroxidases, peroxiredoxins. Biofactors 1999;10:207–209.
   PubMed Web of Science ®Google Scholar
• Skaff O, Pattison DI, Morgan PE, Bachana R, Jain VK, Priyadarsini KI, Davies MJ. Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage. Biochem J 2012;441:305–316.
   PubMed Web of Science ®Google Scholar
• Takahashi K, Cohen HJ. Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes. Blood 1986;68: 640–645.
   PubMed Web of Science ®Google Scholar
• Halliwell B, Gutteridge JMC. Free radicals in biology and medicine. Oxford: Oxford University Press; 2007. pp. 1–704.
   Google Scholar
• Drummond GR, Sobey CG. Endothelial NADPH oxidases: which noxNOx to target in vascular disease? Trends Endocrinol Metabol 2014;25:452–463.
   PubMed Web of Science ®Google Scholar
• Cifuentes-Pagano E, Meijles DN, Pagano PJ. The quest for selective NOx inhibitors and therapeutics: challenges, triumphs and pitfalls. Antiox Redox Signal 2014;20: 2741–2754.
   PubMed Web of Science ®Google Scholar
• Davies MJ, Hawkins CL, Pattison DI, Rees MD. Mammalian heme peroxidases: From molecular mechanisms to health implications. Antiox Redox Signal 2008;10:1199–1234.
   PubMed Web of Science ®Google Scholar
• Hawkins CL, Pattison DI, Davies MJ. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 2003;25:259–274.
   PubMed Web of Science ®Google Scholar
• Pattison DI, Davies MJ. Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Curr Med Chem 2006;13:3271–3290.
   PubMed Web of Science ®Google Scholar
• Barrett TJ, Hawkins CL. Hypothiocyanous acid: benign or deadly? Chem Res Toxicol 2012;25:263–273.
   PubMed Web of Science ®Google Scholar
• Winterbourn CC. Reconciling the chemistry and biology of reactive oxygen species. Nature Chem Biol 2008;4: 278–286.
   PubMed Web of Science ®Google Scholar
• Furtmuller PG, Zederbauer M, Jantschko W, Helm J, Bogner M, Jakopitsch C, Obinger C. Active site structure and catalytic mechanisms of human peroxidases. Arch Biochem Biophys 2006;445:199–213.
   PubMed Web of Science ®Google Scholar
• Stubbe JA. Radicals with a controlled lifestyle. Chem Comm 2003;20:2511–2513.
   Web of Science ®Google Scholar
• Radi R. Peroxynitrite, a stealthy biological oxidant. J Biol Chem 2013;288:26464–26472.
   PubMed Web of Science ®Google Scholar
• Davies MJ, Hawkins CL. EPR spin trapping of protein radicals. Free Radic Biol Med 2004;36:1072–1086.
   PubMed Web of Science ®Google Scholar
• van der Veen BS, de Winther MP, Heeringa P. Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease. Antiox Redox Signal 2009;11:2899–2937.
   PubMed Web of Science ®Google Scholar
• Hondal RJ, Marino SM, Gladyshev VN. Selenocysteine in thiol/disulfide-like exchange reactions. Antiox Redox Signal 2013;18:1675–1689.
   PubMed Web of Science ®Google Scholar
• Jacob C, Giles GI, Giles NM, Sies H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew Chem Int Ed Engl 2003;42:4742–4758.
   PubMed Web of Science ®Google Scholar
• Orian L, Toppo S. Organochalcogen peroxidase mimetics as potential drugs: a long story of a promise still unfulfilled. Free Radic Biol Med 2014;66:65–74.
   PubMed Web of Science ®Google Scholar
• Azad GK, Tomar RS. Ebselen, a promising antioxidant drug: mechanisms of action and targets of biological pathways. Mol Biol Rep 2014;41:4865–4879.
   PubMed Web of Science ®Google Scholar
• Weekley CM, Harris HH. Which form is that? The importance of selenium speciation and metabolism in the prevention and treatment of disease. Chem Soc Rev 2013;42:8870–8894.
   Google Scholar
• Battin EE, Brumaghim JL. Antioxidant activity of sulfur and selenium: a review of reactive oxygen species scavenging, glutathione peroxidase, and metal-binding antioxidant mechanisms. Cell Biochem Biophys 2009;55:1–23.
   PubMed Web of Science ®Google Scholar
• Snider GW, Ruggles E, Khan N, Hondal RJ. Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes. Biochemistry 2013;52:5472–5481.
   PubMed Web of Science ®Google Scholar
• Chandler JD, Nichols DP, Nick JA, Hondal RJ, Day BJ. Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense. J Biol Chem 2013;288: 18421–18428.
   PubMed Web of Science ®Google Scholar
• Zhong L, Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J Biol Chem 2000;275: 18121–1818.
   PubMed Web of Science ®Google Scholar
• Gasdaska JR, Harney JW, Gasdaska PY, Powis G, Berry MJ. Regulation of human thioredoxin reductase expression and activity by 3’-untranslated region selenocysteine insertion sequence and mRNA instability elements. J Biol Chem 1999;274:25379–25385.
   PubMed Web of Science ®Google Scholar
• Martinez J, Lisa S, Sanchez R, Kowalczyk W, Zurita E, Teixido M, et al.Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity. Plos One 2011;6:e27999.
   Web of Science ®Google Scholar
• Nagy P, Karton A, Betz A, Peskin AV, Pace P, O’Reilly RJ, et al.Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study. J Biol Chem 2011;286:18048–18055.
   PubMed Web of Science ®Google Scholar
• Cardey B, Enescu M. Selenocysteine versus cysteine reactivity: a theoretical study of their oxidation by hydrogen peroxide. J Phys Chem A 2007;111:673–678.
   PubMed Web of Science ®Google Scholar
• Padmaja S, Squadrito GL, Lemercier JN, Cueto R, Pryor WA. Rapid oxidation of dl-selenomethionine by peroxynitrite. Free Radic Biol Med 1996;21:317–322.
   PubMed Web of Science ®Google Scholar
• Alvarez B, Ferrer-Sueta G, Freeman BA, Radi R. Kinetics of peroxynitrite reaction with amino acids and human serum albumin. J Biol Chem 1999;274:842–848.
   PubMed Web of Science ®Google Scholar
• Briviba K, Roussyn I, Sharov VS, Sies H. Attenuation of oxidation and nitration reactions of peroxynitrite by selenomethionine, selenocystine and ebselen. Biochem J 1996;319: 13–15.
   PubMed Web of Science ®Google Scholar
• Roussyn I, Briviba K, Masumoto H, Sies H. Selenium-containing compounds protect DNA from single-strand breaks caused by peroxynitrite. Arch Biochem Biophys 1996;330:216–218.
   PubMed Web of Science ®Google Scholar
• Storkey C, Pattison DI, White JM, Schiesser CH, Davies MJ. Preventing protein oxidation with sugars: scavenging of hypohalous acids by 5-selenopyranose and 4-selenofuranose derivatives. Chem Res Toxicol 2012;25:2589–2599.
   PubMed Web of Science ®Google Scholar
• Storkey C, Davies MJ, Pattison DI. Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach. Free Radic Biol Med 2014;73:60–66.
   PubMed Web of Science ®Google Scholar
• Pattison DI, Davies MJ. A kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and the use of 3-bromotyrosine as a marker of oxidative stress. Biochemistry 2004;43: 4799–4809.
   PubMed Web of Science ®Google Scholar
• Carroll L, Pattison DI, Fu S, Schiesser CH, Davies MJ, Hawkins CL. Reactivity of selenium-containing compounds with myeloperoxidase-derived chlorinating oxidants: second-order rate constants and implications for preventing inflammation- induced biological damage. Free Radical Biology and Medicine on 26/3/2015. doi:10.1016/j.freeradbiomed.2015.03.029.
   Google Scholar
• Peskin AV, Winterbourn CC. Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radic Biol Med 2001;30: 572–579.
   PubMed Web of Science ®Google Scholar
• Beal JL, Foster SB, Ashby MT. Hypochlorous acid reacts with the N-terminal methionines of proteins to give dehydromethionine, a potential biomarker for neutrophil-induced oxidative stress. Biochemistry 2009;48: 11142–11148.
   PubMed Web of Science ®Google Scholar
• Peskin AV, Turner R, Maghzal GJ, Winterbourn CC, Kettle AJ. Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils. Biochemistry 2009;48:10175–10182.
   PubMed Web of Science ®Google Scholar
• Krause RJ, Glocke SC, Sicuri AR, Ripp SL, Elfarra AA. Oxidative metabolism of seleno-l-methionine to l-methionine selenoxide by flavin-containing monooxygenases. Chem Res Toxicol 2006;19:1643–1649.
   PubMed Web of Science ®Google Scholar
• Suryo Rahmanto A, Davies MJ. Catalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides. Free Radic Biol Med 2011;51:2288–2299.
   PubMed Web of Science ®Google Scholar
• Mishra B, Priyadarsini KI, Mohan H. Effect of pH on one-electron oxidation chemistry of organoselenium compounds in aqueous solutions. J Phys Chem A 2006;110:1894–1900.
   PubMed Web of Science ®Google Scholar
• Mishra B, Sharma A, Naumov S, Priyadarsini KI. Novel reactions of one-electron oxidized radicals of selenomethionine in comparison with methionine. J Phys Chem B 2009;113:7709–7715.
   PubMed Web of Science ®Google Scholar
• Schoneich C. Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease. Biochim Biophys Acta 2005;1703:111–119.
   PubMed Web of Science ®Google Scholar
• Schoneich C, Pogocki D, Hug GL, Bobrowski K. Free radical reactions of methionine in peptides: Mechanisms relevant to beta-amyloid oxidation and Alzheimer's disease. J Am Chem Soc 2003;125:13700–13713.
   PubMed Web of Science ®Google Scholar
• Hiller KO, Masloch B, Gobl M, Asmus KD. Mechanism of the OH-radical induced oxidation of methionine in aqueous solution. J Am Chem Soc 1981;103:2734–2743.
   Web of Science ®Google Scholar
• Hiller KO, Asmus KD. Formation and reduction reactions of α-amino radicals derived from methionine and its derivatives in aqueous solutions. J Phys Chem 1983;87:3682–3688.
   Web of Science ®Google Scholar
• Priyadarsini KI, Mishra B. Radical cations of some water-soluble organoselenium compounds: insights from pulse radiolysis studies. Radiat Phys Chem 2008;77:1294–1299.
   Web of Science ®Google Scholar
• Priyadarsini KI, Mishra B. A brief account on radiation chemical studies of antioxidants: examples from natural phenols, sulfur and selenium compounds. J Ind Chem Soc 2010;87:147–157.
   Web of Science ®Google Scholar
• Huang ML, Rauk A. Reactions of one-electron-oxidized methionine with oxygen: an ab initio study. J Phys Chem A 2004;108:6222–6230.
   Web of Science ®Google Scholar
• Cardey B, Enescu M. A computational study of thiolate and selenolate oxidation by hydrogen peroxide. Chem Phys Chem 2005;6:1175–1180.
   Web of Science ®Google Scholar
• Skaff O, Pattison DI, Davies MJ. Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance. Biochem J 2009;422:111–117.
   PubMed Web of Science ®Google Scholar
• Koppenol WH, Moreno JJ, Pryor WA, Ischiropoulos H, Beckman JS. Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chem Res Toxicol 1992;5:834–842.
   PubMed Web of Science ®Google Scholar
• Trujillo M, Radi R. Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: new insights into the reaction of peroxynitrite with thiols. Arch Biochem Biophys 2002;397:91–98.
   PubMed Web of Science ®Google Scholar
• Takebe G, Yarimizu J, Saito Y, Hayashi T, Nakamura H, Yodoi J, et al.A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P. J Biol Chem 2002;277:41254–41258.
   PubMed Web of Science ®Google Scholar
• Briviba K, Kissner R, Koppenol WH, Sies H. Kinetic study of the reaction of glutathione peroxidase with peroxynitrite. Chem Res Toxicol 1998;11:1398–1401.
   PubMed Web of Science ®Google Scholar
• Padmaja S, Squadrito GL, Pryor WA. Inactivation of glutathione peroxidase by peroxynitrite. Arch Biochem Biophys 1998;349:1–6.
   PubMed Web of Science ®Google Scholar
• Nucifora G, Smaller B, Remko R, Avery EC. Transient radicals of DNA bases by pulse radiolysis. Effects of cysteine and cysteamine as radioprotectors. Radiat Res 1972;49: 96–111.
   PubMed Web of Science ®Google Scholar
• Eriksen TE, Fransson G. Formation of reducing radicals on radiolysis of glutathione and some related compounds in aqueous solution. J Chem Soc Perkin Trans 2 1988: 1117–1122.
   Google Scholar
• Steinmann D, Nauser T, Beld J, Tanner M, Gunther D, Bounds PL, Koppenol WH. Kinetics of tyrosyl radical reduction by selenocysteine. Biochemistry 2008;47:9602–9607.
   PubMed Web of Science ®Google Scholar
• Gebicki JM, Nauser T, Domazou A, Steinmann D, Bounds PL, Koppenol WH. Reduction of protein radicals by GSH and ascorbate: potential biological significance. Amino Acids 2010;39:1131–1137.
   PubMed Web of Science ®Google Scholar
• Turell L, Botti H, Carballal S, Ferrer-Sueta G, Souza JM, Duran R, et al.Reactivity of sulfenic acid in human serum albumin. Biochemistry 2008;47:358–367.
   PubMed Web of Science ®Google Scholar
• Barrett TJ, Pattison DI, Leonard SE, Carroll KS, Davies MJ, Hawkins CL. Inactivation of thiol-dependent enzymes by hypothiocyanous acid: Role of sulfenyl thiocyanate and sulfenic acid intermediates. Free Radic Biol Med 2012;52:1075–1085.
   PubMed Web of Science ®Google Scholar
• Algunindigue Nimmo SL, Lemma K, Ashby MT. Reactions of cysteine sulfenyl thiocyanate with thiols to give unsymmetrical disulfides. Heteroatom Chem 2007;18:467–471.
   Web of Science ®Google Scholar
• Ashby MT, Aneetha H. Reactive sulfur species: aqueous chemistry of sulfenyl thiocyanates. J Am Chem Soc 2004;126:10216–10217.
   PubMed Web of Science ®Google Scholar
• Lemma K, Ashby MT. Reactive sulfur species: kinetics and mechanism of the equilibrium between cysteine sulfenyl thiocyanate and cysteine thiosulfinate ester in acidic aqueous solution. J Org Chem 2008;73:3017–3023.
   PubMed Web of Science ®Google Scholar
• Nagy P, Ashby MT. Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid. J Am Chem Soc 2007;129: 14082–14091.
   PubMed Web of Science ®Google Scholar
• Nagy P, Lemma K, Ashby MT. Reactive sulfur species: kinetics and mechanisms of the reaction of cysteine thiosulfinate ester with cysteine to give cysteine sulfenic acid. J Org Chem 2007;72:8838–8846.
   PubMed Web of Science ®Google Scholar
• Cho CS, Lee S, Lee GT, Woo HA, Choi EJ, Rhee SG. Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells. Antiox Redox Signal 2010;12:1235–1246.
   PubMed Web of Science ®Google Scholar
• Hondal RJ, Ruggles EL. Differing views of the role of selenium in thioredoxin reductase. Amino Acids 2011;41: 73–89.
   PubMed Web of Science ®Google Scholar
• Zielinski Z, Presseau N, Amorati R, Valgimigli L, Pratt DA. Redox chemistry of selenenic acids and the insight it brings on transition state geometry in the reactions of peroxyl radicals. J Am Chem Soc 2014;136:1570–1578.
   PubMed Web of Science ®Google Scholar
• Li F, Liu J, Rozovsky S. Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment. Free Radic Biol Med 2014;76:127–135.
   PubMed Web of Science ®Google Scholar
• Okeley NM, Zhu Y, van Der Donk WA. Facile chemoselective synthesis of dehydroalanine-containing peptides. Org Lett 2000;2:3603–3606.
   PubMed Web of Science ®Google Scholar
• Wang J, Schiller SM, Schultz PG. A biosynthetic route to dehydroalanine-containing proteins. Angew Chem Int Ed Engl 2007;46:6849–6851.
   PubMed Web of Science ®Google Scholar
• Guo J, Wang J, Lee JS, Schultz PG. Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins. Angew Chem Int Ed Engl 2008;47:6399–6401.
   PubMed Web of Science ®Google Scholar
• Hashimoto K, Sakai M, Okuno T, Shirahama H. Beta-phenylselenoalanine as a dehydroalanine precursor-efficient synthesis of alternariolide (AM-toxin I). Chem Commun 1996:1139–1140.
   Web of Science ®Google Scholar
• Sakai M, Hashimoto K, Shirahama H. Synthesis of optically pure beta-phenylselenoalanine through serine-beta-lactone: a useful precursor of dehydroalanine. Heterocycles 1997;44:319–324.
   Web of Science ®Google Scholar
• Nauser T, Steinmann D, Koppenol WH. Why do proteins use selenocysteine instead of cysteine? Amino Acids 2012;42: 39–44.
   PubMed Web of Science ®Google Scholar
• Zhang XJ, Zhang N, Schuchmann HP, Vonsonntag C. Pulse-radiolysis of 2-mercaptoethanol in oxygenated aqueous-solution - generation and reactions of the thiylperoxyl radical. J Phys Chem 1994;98:6541–6547.
   Web of Science ®Google Scholar
• Zhao R, Lind J, Merenyi G, Eriksen TE. Kinetics of one-electron oxidation of thiols and hydrogen abstraction by thiyl radicals from alpha-amino C-H bonds. J Am Chem Soc 1994;116:12010–12015.
   Web of Science ®Google Scholar
• Willson RL. Pulse radiolysis studies of electron transfer in aqueous disulphide solutions. J Chem Soc Chem Commun 1970:1425.
   Google Scholar
• Winterbourn CC. Superoxide as an intracellular radical sink. Free Radic Biol Med 1993;14:85–90.
   PubMed Web of Science ®Google Scholar
• Koppenol WH. A thermodynamic appraisal of the radical sink hypothesis. Free Radic Biol Med 1993;14:91–94.
   PubMed Web of Science ®Google Scholar
• Davies MJ, Hawkins CL. Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates. Free Radic Res 2000;33: 719–729.
   PubMed Web of Science ®Google Scholar
• Nauser T, Koppenol WH, Schoneich C. Reversible hydrogen transfer reactions in thiyl radicals from cysteine and related molecules: Absolute kinetics and equilibrium constants determined by pulse radiolysis. J Phys Chem B 2012;116: 5329–5341.
   PubMed Web of Science ®Google Scholar
• Armstrong DA. Applications of pulse-radiolysis for the study of short-lived sulfur species. In: Chatgilialoglu C, Asmus KD (eds.). Sulfur-centered reactive intermediates in chemistry and biology. New York: Springer; 1990. pp. 121–134.
   Google Scholar
• Wardman P, von Sonntag C. Kinetic factors that control the fate of thiyl radicals in cells. Methods Enzymol 1995;251: 31–45.
   PubMed Web of Science ®Google Scholar
• Ferreri C, Kratzsch S, Landi L, Brede O. Thiyl radicals in biosystems: Effects on lipid structures and metabolisms. Cell Mol Life Sci 2005;62:834–847.
   PubMed Web of Science ®Google Scholar
• Kratzsch S, Drossler K, Sprinz H, Brede O. Thiyl radicals in biosystems: Inhibition of the prostaglandin metabolism by the cis-trans-isomerization of arachidonic acid double bonds. Arch Biochem Biophys 2003;416:238–248.
   PubMed Web of Science ®Google Scholar
• Chatgilialoglu C, Ferreri C, Melchiorre M, Sansone A, Torreggiani A. Lipid geometrical isomerism: from chemistry to biology and diagnostics. Chem Rev 2014;114:255–284.
   PubMed Web of Science ®Google Scholar
• Lykakis IN, Ferreri C, Chatgilialoglu C. The sulfhydryl radical (HS•/S•−): a contender for the isomerization of double bonds in membrane lipids. Angew Chem Int Ed Engl 2007;46:1914–1916.
   PubMed Web of Science ®Google Scholar
• Nauser T, Steinmann D, Grassi G, Koppenol WH. Why selenocysteine replaces cysteine in thioredoxin reductase: a radical hypothesis. Biochemistry 2014;53:5017–5022.
   PubMed Web of Science ®Google Scholar
• Mozziconacci O, Kerwin BA, Schoneich C. Reversible hydrogen transfer reactions of cysteine thiyl radicals in peptides: the conversion of cysteine into dehydroalanine and alanine, and of alanine into dehydroalanine. J Phys Chem B 2011;115:12287–12305.
   PubMed Web of Science ®Google Scholar
• Naidu BN, Sorenson ME, Connolly TP, Ueda Y. Michael addition of amines and thiols to dehydroalanine amides: A remarkable rate acceleration in water. J Org Chem 2003;68:10098–10102.
   PubMed Web of Science ®Google Scholar
• Linetsky M, LeGrand RD. Glutathionylation of lens proteins through the formation of thioether bond. Mol Cell Biochem 2005;272:133–144.
   PubMed Web of Science ®Google Scholar
• Linetsky M, Hill JMW, LeGrand RD, Hu F. Dehydroalanine crosslinks in human lens. Exp Eye Res 2004;79:499–512.
   PubMed Web of Science ®Google Scholar
• Bar-Or R, Rael LT, Bar-Or D. Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin. Rapid Commun Mass Spectr 2008;22:711–716.
   PubMed Web of Science ®Google Scholar
• Jeong J, Jung Y, Na S, Jeong J, Lee E, Kim M-S, et al.Novel oxidative modifications in redox-active cysteine residues. Mol Cell Proteom 2011;10:M110.000513.
   Web of Science ®Google Scholar
• Cho C-S, Lee S, Lee GT, Woo HA, Choi E-J, Rhee SG. Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells. Antiox Redox Signal 2010;12:1235–1246.
   PubMed Web of Science ®Google Scholar
• Ma S, Caprioli RM, Hill KE, Burk RF. Loss of selenium from selenoproteins: Conversion of selenocysteine to dehydroalanine in vitro. J Am Soc Mass Spectrom 2003;14: 593–600.
   PubMed Web of Science ®Google Scholar
• Townsend DM, Lushchak VI, Cooper AJL. A comparison of reversible versus irreversible protein glutathionylation. In: Townsend DM, Tew KD (eds). Redox and Cancer pt A, Volume 122, Advances in Cancer Research. Amsterdam: Elsevier; 2014. pp. 177–198.
   Google Scholar
• Packer L, Witt EH, Tritschler HJ. Alpha-lipoic acid as a biological antioxidant. Free Radic Biol Med 1995;19:227–250.
   PubMed Web of Science ®Google Scholar
• Bhabak KP, Mugesh G. Functional mimics of glutathione peroxidase: bioinspired synthetic antioxidants. Acc Chem Res 2010;43:1408–1419.
   PubMed Web of Science ®Google Scholar
• de Bem AF, Fiuza B, Calcerrada P, Brito PM, Peluffo G, Dinis TC, et al.Protective effect of diphenyl diselenide against peroxynitrite-mediated endothelial cell death: a comparison with ebselen. Nitric Oxide 2013;31:20–30.
   PubMed Web of Science ®Google Scholar
• Kumar BS, Kunwar A, Ahmad A, Kumbhare LB, Jain VK, Priyadarsini KI. In vitro radioprotection studies of organoselenium compounds: differences between mono- and diselenides. Radiat Environ Biophys 2009;48:379–384.
   PubMed Web of Science ®Google Scholar
• Kunwar A, Bansal P, Kumar SJ, Bag PP, Paul P, Reddy ND, et al.In vivo radioprotection studies of 3,3’-diselenodipropionic acid, a selenocystine derivative. Free Radic Biol Med 2010;48:399–410.
   PubMed Web of Science ®Google Scholar
• Mishra B, Kumbhare LB, Jain VK, Priyadarsini KI. Pulse radiolysis studies on reactions of hydroxyl radicals with selenocystine derivatives. J Phys Chem B 2008;112:4441–4446.
   PubMed Web of Science ®Google Scholar
• Mugesh G, Panda A, Singh HB, Punekar NS, Butcher RJ. Glutathione peroxidase-like antioxidant activity of diaryl diselenides: a mechanistic study. J Am Chem Soc 2001;123:839–850.
   PubMed Web of Science ®Google Scholar
• Stefanello ST, Prestes AS, Ogunmoyole T, Salman SM, Schwab RS, Brender CR, et al.Evaluation of in vitro antioxidant effect of new mono and diselenides. Toxicol In Vitro 2013;27:1433–1439.
   PubMed Web of Science ®Google Scholar
• Kunwar A, Mishra B, Barik A, Kumbhare LB, Pandey R, Jain VK, Priyadarsini KI. 3,3’-diselenodipropionic acid, an efficient peroxyl radical scavenger and a GPx mimic, protects erythrocytes (RBCs) from AAPH-induced hemolysis. Chem Res Toxicol 2007;20:1482–1487.
   PubMed Web of Science ®Google Scholar
• Yoshida S, Kumakura F, Komatsu I, Arai K, Onuma Y, Hojo H, et al.Antioxidative glutathione peroxidase activity of selenoglutathione. Angew Chemie Int Ed Engl 2011;50:2125–2128.
   PubMed Web of Science ®Google Scholar
• Pattison DI, Davies MJ. Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem Res Toxicol 2001;14:1453–1464.
   PubMed Web of Science ®Google Scholar
• Masuda T, Nakano S, Kondo M. Rate constants for the reactions of OH radicals with the enzyme proteins as determined by the p-nitrosodimethylaniline method. J Radiat Res 1973;14:339–345.
   PubMedGoogle Scholar
• Quintiliani M, Badiello R, Tamba M, Esfandi A, Gorin G. Radiolysis of glutathione in oxygen-containing solutions of pH7. Int J Radiat Biol Phys Chem Med 1977;32:195–202.
   PubMed Web of Science ®Google Scholar
• Finley JW, Wheeler EL, Witt SC. Oxidation of glutathione by hydrogen-peroxide and other oxidizing-agents. J Agric Food Chem 1981;29:404–407.
   PubMed Web of Science ®Google Scholar
• Devasagayam TPA, Sundquist AR, Di Mascio P, Kaiser S, Sies H. Activity of thiols as singlet molecular-oxygen quenchers. J Photochem Photobiol B 1991;9:105–116.
   PubMed Web of Science ®Google Scholar
• Clennan EL, Wang DY, Clifton C, Chen MF. Geometry-dependent quenching of singlet oxygen by dialkyl disulfides. J Am Chem Soc 1997;119:9081–9082.
   Web of Science ®Google Scholar
• Okamoto T, Akaike T, Sawa T, Miyamoto Y, van der Vliet A, Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 2001;276:29596–29602.
   PubMed Web of Science ®Google Scholar
• Giles GI, Tasker KM, Collins C, Giles NM, O’Rourke E, Jacob C. Reactive sulphur species: An in vitro investigation of the oxidation properties of disulphide S-oxides. Biochem J 2002;364:579–585.
   PubMed Web of Science ®Google Scholar
• Giles GI, Tasker KM, Jacob C. Oxidation of biological thiols by highly reactive disulfide-S-oxides. Gen Physiol Biophys 2002;21:65–72.
   PubMed Web of Science ®Google Scholar
• Huang K-P, Huang FL. Glutathionylation of proteins by glutathione disulfide S-oxide. Biochem Pharmacol 2002;64:1049–1056.
   PubMed Web of Science ®Google Scholar
• Huang K-P, Huang FL, Shetty PK, Yergey AL. Modification of protein by disulfide S-monoxide and disulfide S-dioxide: distinctive effects on PKC. Biochemistry 2007;46:1961–1971.
   PubMed Web of Science ®Google Scholar
• Hu Y, Wang TW, Liao XY, Du GC, Chen JA, Xu JG. Anti-oxidative stress and beyond: Multiple functions of the protein glutathionylation. Protein Pept Lett 2010;17:1234–1244.
   PubMed Web of Science ®Google Scholar
• Prabhu PC, Adhikari B, Phadnis PP, Chakraborty S, Jain VK, Priyadarsini KI. In vitro antioxidant studies on diselenodinicotinamide: a potent GPx mimic. Indian J Chem A 2014;53:781–786.
   Google Scholar
• Prabhu P, Singh BG, Noguchi M, Phadnis PP, Jain VK, Iwaoka M, Priyadarsini KI. Stable selones in glutathione-peroxidase-like catalytic cycle of selenonicotinamide derivative. Org Biomol Chem 2014;12:2404–2412.
   PubMed Web of Science ®Google Scholar
• Bhuyan BJ, Lamani DS, Mugesh G, Wirth T. Current research on mimics and models of selenium-containing antioxidants. In: Devillanova FA, Du Mont WW (eds.). Handbook of Chalcogen Chemistry: New Perspectives in Sulfur, Selenium and Tellurium, Vol. 2. 2nd ed. Cambridge, UK: Royal Society of Chemistry; 2013. pp. 25–46.
   Google Scholar
• Iwaoka M, Tomoda S. A model study on the effect of an amino group on the antioxidant activity of glutathione peroxidase. J Am Chem Soc 1994;116:2557–2561.
   Web of Science ®Google Scholar
• Morgenstern R, Cotgreave IA, Engman L. Determination of the relative contributions of the diselenide and selenol forms of ebselen in the mechanism of its glutathione peroxidase-like activity. Chem Biol Interact 1992;84:77–84.
   PubMed Web of Science ®Google Scholar
• Masumoto H, Kissner R, Koppenol WH, Sies H. Kinetic study of the reaction of ebselen with peroxynitrite. FEBS Lett 1996;398:179–182.
   PubMed Web of Science ®Google Scholar
• Scurlock R, Rougee M, Bensasson RV, Evers M, Dereu N. Deactivation of singlet molecular oxygen by organo-selenium compounds exhibiting glutathione peroxidase activity and by sulfur-containing homologs. Photochem Photobiol 1991;54:733–736.
   PubMed Web of Science ®Google Scholar
• Selvakumar K, Shah P, Singh HB, Butcher RJ. Synthesis, structure, and glutathione peroxidase-like activity of amino acid containing ebselen analogues and diaryl diselenides. Chem Eur J 2011;17:12741–12755.
   PubMed Web of Science ®Google Scholar
• Balkrishna SJ, Kumar S, Azad GK, Bhakuni BS, Panini P, Ahalawat N, et al.An ebselen like catalyst with enhanced GPx activity via a selenol intermediate. Org Biomol Chem 2014;12:1215–1219.
   PubMed Web of Science ®Google Scholar
• Satheeshkumar K, Mugesh G. Synthesis and antioxidant activity of peptide-based ebselen analogues. Chem Eur J 2011;17:4849–4857.
   PubMed Web of Science ®Google Scholar
• Prabhu P, Bag PP, Singh BG, Hodage A, Jain VK, Iwaoka M, Priyadarsini KI. Effect of functional groups on antioxidant properties of substituted selenoethers. Free Radic Res 2011;45:461–468.
   PubMed Web of Science ®Google Scholar
• Barik A, Singh BG, Sharma A, Jain VK, Priyadarsini KI. Pulse radiolysis studies of 3,5-dimethyl pyrazole derivatives of selenoethers. J Phys Chem A 2014;118:10179–10187.
   PubMed Web of Science ®Google Scholar
• Singh BG, Thomas E, Kumakura F, Dedachi K, Iwaoka M, Priyadarsini KI. One-electron redox processes in a cyclic selenide and a selenoxide: a pulse radiolysis study. J Phys Chem A 2010;114:8271–8277.
   PubMed Web of Science ®Google Scholar
• Kumakura F, Mishra B, Priyadarsini KI, Iwaoka M. A water-soluble cyclic selenide with enhanced glutathione peroxidase-like catalytic activity. Eur J Org Chem 2010:440–445.
   Web of Science ®Google Scholar
• Storkey C, Davies MJ, White JM, Schiesser CH. Synthesis and antioxidant capacity of 5-selenopyranose derivatives. Chem Commun 2011;47:9693–9695.
   PubMed Web of Science ®Google Scholar
• Brot N, Weissbach L, Werth J, Weissbach H. Enzymatic reduction of protein-bound methionine sulfoxide. Proc Natl Acad Sci USA 1981;78:2155–2158.
   PubMed Web of Science ®Google Scholar
• Grimaud R, Ezraty B, Mitchell JK, Lafitte D, Briand C, Derrick PJ, Barras F. Repair of oxidized proteins – identification of a new methionine sulfoxide reductase. J Biol Chem 2001;276:48915–48920.
   PubMed Web of Science ®Google Scholar
• Sharov VS, Ferrington DA, Squier TC, Schoneich C. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett 1999;455:247–250.
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Poston JM, Berlett BS, Nosworthy NJ, Szczepanowski R, Stadtman ER. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J Biol Chem 2000;275:14167–14172.
   PubMed Web of Science ®Google Scholar
• Tarrago L, Kaya A, Weerapana E, Marino SM, Gladyshev VN. Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding. J Biol Chem 2012;287:24448–24459.
   PubMed Web of Science ®Google Scholar
• Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, Lowther WT. Free methionine-®-sulfoxide reductase from Escherichia coli reveals a new GAF domain function. Proc Natl Acad Sci USA 2007;104:9597–9602.
   PubMed Web of Science ®Google Scholar
• Etienne F, Spector D, Brot N, Weissbach H. A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide. Biochem Biophys Res Commun 2003;300:378–382.
   PubMed Web of Science ®Google Scholar
• Assmann A, Briviba K, Sies H. Reduction of methionine selenoxide to selenomethionine by glutathione. Arch Biochem Biophys 1998;349:201–203.
   PubMed Web of Science ®Google Scholar
• Maiorino M, Roveri A, Coassin M, Ursini F. Kinetic mechanism and substrate specificity of glutathione peroxidase activity of ebselen (PZ51). Biochem Pharmacol 1988;37: 2267–2271.
   PubMed Web of Science ®Google Scholar
• Müller A, Cadenas E, Graf P, Sies H. A novel biologically active seleno-organic compound: Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ51 (Ebselen). Biochem Pharmacol 1984;33:3235–3239.
   PubMed Web of Science ®Google Scholar
• Krause RJ, Elfarra AA. Reduction of l-methionine selenoxide to seleno-l-methionine by endogenous thiols, ascorbic acid, or methimazole. Biochem Pharmacol 2009;77: 134–140.
   PubMed Web of Science ®Google Scholar
• Pullar JM, Winterbourn CC, Vissers M. Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. Am J Physiol Heart Circ Physiol 1999;277:H1505–H1512.
   PubMed Web of Science ®Google Scholar
• Vissers M, Winterbourn CC. Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid. Biochem J 1995;307:57–62.
   PubMed Web of Science ®Google Scholar
• Smit M, Anderson R. Inhibition of mitogen-activated proliferation of human lymphocytes by hypochlorous acid in vitro: Protection and reversal by ascorbate and cysteine. Inflamm Res 1990;30:338–343.
   Google Scholar
• Smit M, Anderson R. Biochemical mechanisms of hydrogen peroxide-and hypochlorous acid-mediated inhibition of human mononuclear leukocyte functions in vitro: Protection and reversal by anti-oxidants. Inflamm Res 1992;36:58–65.
   Google Scholar
• Fu X, Mueller DM, Heinecke JW. Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: a potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase. Biochemistry 2002;41:1293–1301.
   PubMed Web of Science ®Google Scholar
• Lloyd MM, Grima MA, Rayner BS, Hadfield KA, Davies MJ, Hawkins CL. Comparative reactivity of the myeloperoxidase-derived oxidants hypochlorous acid and hypothiocyanous acid with human coronary artery endothelial cells. Free Radic Biol Med 2013;65:1352–1362.
   PubMed Web of Science ®Google Scholar
• Summers FA, Quigley AF, Hawkins CL. Identification of proteins susceptible to thiol oxidation in endothelial cells exposed to hypochlorous acid and N-chloramines. Biochem Biophys Res Commun 2012;425:157–161.
   PubMed Web of Science ®Google Scholar
• Bozonet SM, Scott-Thomas AP, Nagy P, Vissers MC. Hypothiocyanous acid is a potent inhibitor of apoptosis and caspase 3 activation in endothelial cells. Free Radic Biol Med 2010;49:1054–1063.
   PubMed Web of Science ®Google Scholar
• Pullar JM, Vissers MCM, Winterbourn CC. Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide. J Biol Chem 2001;276:22120–22125.
   PubMed Web of Science ®Google Scholar
• Summers FA, Morgan PE, Davies MJ, Hawkins CL. Identification of plasma proteins that are susceptible to thiol oxidation by hypochlorous acid and N-chloramines. Chem Res Toxicol 2008;21:1832–1840.
   PubMed Web of Science ®Google Scholar
• Peskin AV, Winterbourn CC. Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase. Free Radic Biol Med 2006;40:45–53.
   PubMed Web of Science ®Google Scholar
• Chae HZ, Chung SJ, Rhee SG. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 1994;269: 27670–27678.
   PubMed Web of Science ®Google Scholar
• Rotruck J, Pope A, Ganther H, Swanson A, Hafeman D, Hoekstra W. Selenium: Biochemical role as a component of glutathione peroxidase. Science 1973;179:588.
   PubMed Web of Science ®Google Scholar
• Stadtman T. Biosynthesis and function of selenocysteine-containing enzymes. J Biol Chem 1991;266:16257–16260.
   PubMed Web of Science ®Google Scholar
• Zhong L, Holmgren A. Mammalian thioredoxin reductases as hydroperoxide reductases. Methods Enzymol 2002;347: 236–243.
   PubMed Web of Science ®Google Scholar
• Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 2003;300:653–656.
   PubMed Web of Science ®Google Scholar
• Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, Rhee SG. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 2002;277:38029–38036.
   PubMed Web of Science ®Google Scholar
• Bjornstedt M, Kumar S, Bjorkhem L, Spyrou G, Holmgren A. Selenium and the thioredoxin and glutaredoxin systems. Biomed Environ Sci 1997;10:271–279.
   PubMedGoogle Scholar
• Holmgren A. Thioredoxin. Annu Rev Biochem 1985;54: 237–271.
   PubMed Web of Science ®Google Scholar
• Holmgren A, Lu J. Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem Biophys Res Commun 2010;396:120–124.
   PubMed Web of Science ®Google Scholar
• Holmgren A. Thioredoxin .6. Amino acid sequence of protein from Escherichia coli B. Eur J Biochem 1968;6:475.
   Google Scholar
• Weichsel A, Gasdaska JR, Powis G, Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 1996;4:735–751.
   PubMed Web of Science ®Google Scholar
• Zhong L, Arner ES, Holmgren A. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc Natl Acad Sci USA 2000;97:5854–5859.
   PubMed Web of Science ®Google Scholar
• Gladyshev VN, Jeang KT, Stadtman TC. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci USA 1996;93: 6146–6151.
   PubMed Web of Science ®Google Scholar
• Eckenroth B, Harris K, Turanov AA, Gladyshev VN, Raines RT, Hondal RJ. Semisynthesis and characterization of mammalian thioredoxin reductase. Biochemistry 2006;45: 5158–5170.
   PubMed Web of Science ®Google Scholar
• Winterbourn CC, Hampton MB. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 2008;45: 549–561.
   PubMed Web of Science ®Google Scholar
• Forman HJ, Fukuto JM, Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 2004;287:C246–C256.
   PubMed Web of Science ®Google Scholar
• Rosen H, Klebanoff SJ, Wang Y, Brot N, Heinecke JW, Fu X. Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils. Proc Natl Acad Sci USA 2009;106:18686–18691.
   PubMed Web of Science ®Google Scholar
• Reddy VY, Desrochers PE, Pizzo SV, Gonias SL, Sahakian JA, Levine RL, Weiss SJ. Oxidative dissociation of human α(2)-macroglobulin tetramers into dysfunctional dimers. J Biol Chem 1994;269:4683–4691.
   PubMed Web of Science ®Google Scholar
• Wu SM, Pizzo SV. Mechanism of hypochlorite-mediated inactivation of proteinase inhibition by α(2)-macroglobulin. Biochemistry 1999;38:13983–13990.
   PubMed Web of Science ®Google Scholar
• Levine RL, Berlett BS, Moskovitz J, Mosoni L, Stadtman ER. Methionine residues may protect proteins from critical oxidative damage. Mech Age Dev 1999;107:323–332.
   PubMed Web of Science ®Google Scholar
• Luo S, Levine RL. Methionine in proteins defends against oxidative stress. FASEB J 2009;23:464–472.
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Bar-Noy S, Williams WM, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 2001;98:12920–12925.
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Berlett BS, Poston JM, Stadtman ER. The yeast peptide methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci USA 1997;94:9585–9589.
   PubMed Web of Science ®Google Scholar
• Cabreiro F, Picot CR, Perichon M, Castel J, Friguet B, Petropoulos I. Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage. J Biol Chem 2008;283:16673–16681.
   PubMed Web of Science ®Google Scholar
• Ruan H, Tang XD, Chen ML, Joiner MA, Sun G, Brot N, et al.High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002;99:2748–2753.
   PubMed Web of Science ®Google Scholar
• Kigawa T, Yamaguchi-Nunokawa E, Kodama K, Matsuda T, Yabuki T, Matsuda N, et al.Selenomethionine incorporation into a protein by cell-free synthesis. J Struct Func Genom 2002;2:29–35.
   PubMedGoogle Scholar
• Francoleon NE, Carrington SJ, Fukuto JM. The reaction of H2S with oxidized thiols: Generation of persulfides and implications to H2S biology. Arch Biochem Biophys 2011;516:146–153.
   PubMed Web of Science ®Google Scholar
• Li Q, Lancaster JR Jr. Chemical foundations of hydrogen sulfide biology. Nitric Oxide 2013;35:21–34.
   PubMed Web of Science ®Google Scholar
• Mueller EG. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2006;2:185–194.
   PubMed Web of Science ®Google Scholar
• Pan J, Carroll KS. Persulfide reactivity in the detection of protein S-sulfhydration. ACS Chem Biol 2013;8: 1110–1116.
   PubMed Web of Science ®Google Scholar
• Ida T, Sawa T, Ihara H, Tsuchiya Y, Watanabe Y, Kumagai Y, et al.Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling. Proc Natl Acad Sci USA 2014;111:7606–7611.
   PubMed Web of Science ®Google Scholar
• Miranda KM, Wink DA. Persulfides and the cellular thiol landscape. Proc Natl Acad Sci USA 2014;111:7505–7506.
   PubMed Web of Science ®Google Scholar
• Westley J. Rhodanese. Adv Enzymol Mol Biol 1973;39: 327–368.
   PubMedGoogle Scholar
• Toohey JI, Cooper AJ. Thiosulfoxide (sulfane) sulfur: new chemistry and new regulatory roles in biology. Molecules 2014;19:12789–12813.
   PubMed Web of Science ®Google Scholar
• Lima CD. Analysis of the E. coli NifS CsdB protein at 2.0 Å reveals the structural basis for perselenide and persulfide intermediate formation. J Mol Biol 2002;315:1199–1208.
   PubMed Web of Science ®Google Scholar
• Ogasawara Y, Lacourciere G, Stadtman TC. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system. Proc Natl Acad Sci USA 2001;98: 9494–9498.
   PubMed Web of Science ®Google Scholar
• Paulsen CE, Carroll KS. Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery. Chem Rev 2013;113:4633–4679.
   PubMed Web of Science ®Google Scholar
• Huang Z, Rose AH, Hoffmann PR. The role of selenium in inflammation and immunity: from molecular mechanisms to therapeutic opportunities. Antiox Redox Signal 2012;16: 705–743.
   PubMed Web of Science ®Google Scholar
• Rayman MP. Selenium and human health. Lancet 2012;379:1256–1268.
   PubMed Web of Science ®Google Scholar
• Roman M, Jitaru P, Barbante C. Selenium biochemistry and its role for human health. Metallomics 2014;6:25–54.
   PubMed Web of Science ®Google Scholar
• Sanmartin C, Plano D, Font M, Palop JA. Selenium and clinical trials: new therapeutic evidence for multiple diseases. Curr Med Chem 2011;18:4635–4650.
   PubMed Web of Science ®Google Scholar
• Steinbrenner H, Speckmann B, Sies H. Toward understanding success and failures in the use of selenium for cancer prevention. Antiox Redox Signal 2013;19:181–191.
   PubMed Web of Science ®Google Scholar
• Chakraborty S, Yadav SK, Subramanian M, Priyadarsini KI, Iwaoka M, Chattopadhyay S. dl-trans-3,4-dihydroxy-1-selenolane (DHSred) accelerates healing of indomethacin-induced stomach ulceration in mice. Free Radic Res 2012;46: 1378–1386.
   PubMed Web of Science ®Google Scholar
• Kunwar A, Jain VK, Priyadarsini KI, Haston CK. A selenocysteine derivative therapy affects radiation-induced pneumonitis in the mouse. Am J Respir Cell Mol Biol 2013;49:654–661.
   PubMed Web of Science ®Google Scholar
• Hort MA, Straliotto MR, Netto PM, da Rocha JB, de Bem AF, Ribeiro-do-Valle RM. Diphenyl diselenide effectively reduces atherosclerotic lesions in LDLr -/- mice by attenuation of oxidative stress and inflammation. J Cardiovasc Pharmacol 2011;58:91–101.
   PubMed Web of Science ®Google Scholar
• Weng Y, Song Q, Zhou Y, Zhang L, Wang J, Chen J, et al.Immobilization of selenocystamine on TiO2 surfaces for in situ catalytic generation of nitric oxide and potential application in intravascular stents. Biomaterials 2011;32:1253–1263.
   PubMed Web of Science ®Google Scholar
• Loeschner K, Hadrup N, Hansen M, Pereira SA, Gammelgaard B, Moller LH, et al.Absorption, distribution, metabolism and excretion of selenium following oral administration of elemental selenium nanoparticles or selenite in rats. Metallomics 2014;6:330–337.
   PubMed Web of Science ®Google Scholar
• Garcia-Sevillano MA, Garcia-Barrera T, Gomez-Ariza JL. Development of a new column switching method for simultaneous speciation of selenometabolites and selenoproteins in human serum. J Chromatogr A 2013;1318:171–179.
   PubMed Web of Science ®Google Scholar
• Ogra Y, Anan Y. Selenometabolomics explored by speciation. Biol Pharm Bull 2012;35:1863–1869.
   PubMed Web of Science ®Google Scholar
• Weekley CM, Aitken JB, Vogt S, Finney LA, Paterson DJ, de Jonge MD, et al.Uptake, distribution, and speciation of selenoamino acids by human cancer cells: X-ray absorption and fluorescence methods. Biochemistry 2011;50:1641–1650.
   PubMed Web of Science ®Google Scholar
• Weekley CM, Aitken JB, Vogt S, Finney LA, Paterson DJ, de Jonge MD, et al.Metabolism of selenite in human lung cancer cells: X-ray absorption and fluorescence studies. J Am Chem Soc 2011;133:18272–18279.
   PubMed Web of Science ®Google Scholar
• Weekley CM, Aitken JB, Finney L, Vogt S, Witting PK, Harris HH. Selenium metabolism in cancer cells: The combined application of XAS and XFM techniques to the problem of selenium speciation in biological systems. Nutrients 2013;5:1734–1756.
   PubMed Web of Science ®Google Scholar
• Shanu A, Groebler L, Kim HB, Wood S, Weekley CM, Aitken JB, et al.Selenium inhibits renal oxidation and inflammation but not acute kidney injury in an animal model of rhabdomyolysis. Antiox Redox Signal 2013;18:756–769.
   PubMed Web of Science ®Google Scholar
• Weekley CM, Aitken JB, Witting PK, Harris HH. XAS studies of Se speciation in selenite-fed rats. Metallomics 2014;6:2193–2203.
   PubMed Web of Science ®Google Scholar