{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,19]],"date-time":"2026-05-19T03:56:54Z","timestamp":1779163014726,"version":"3.51.4"},"reference-count":42,"publisher":"Elsevier BV","issue":"3-4","license":[{"start":{"date-parts":[[1999,8,1]],"date-time":"1999-08-01T00:00:00Z","timestamp":933465600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Free Radical Biology and Medicine"],"published-print":{"date-parts":[[1999,8]]},"DOI":"10.1016\/s0891-5849(99)00051-9","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T18:01:10Z","timestamp":1027620070000},"page":"322-328","source":"Crossref","is-referenced-by-count":716,"title":["Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide"],"prefix":"10.1016","volume":"27","author":[{"given":"Christine C.","family":"Winterbourn","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diana","family":"Metodiewa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0891-5849(99)00051-9_BIB1","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/0163-7258(90)90045-4","article-title":"Glutathione-dependent protection against oxidative injury","volume":"47","author":"Shan","year":"1990","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB2","doi-asserted-by":"crossref","first-page":"4349","DOI":"10.1016\/0006-2952(89)90641-2","article-title":"Reduced glutathione in combination with superoxide dismutase as an important biological antioxidant defense mechanism","volume":"38","author":"Munday","year":"1989","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB3","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1146\/annurev.bi.54.070185.001513","article-title":"Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation","volume":"54","author":"Ziegler","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB4","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/S0891-5849(96)00501-1","article-title":"Redox regulation of NF-kappa \u03b2 activation","volume":"22","author":"Flohe","year":"1997","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB5","doi-asserted-by":"crossref","first-page":"5314","DOI":"10.1002\/j.1460-2075.1996.tb00916.x","article-title":"Dephosphorylation of tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents","volume":"15","author":"Knebel","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB6","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1096\/fasebj.10.7.8635688","article-title":"Antioxidant and redox regulation of gene transcription","volume":"10","author":"Sen","year":"1996","journal-title":"FASEB J"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB7","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/0891-5849(94)90042-6","article-title":"Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells","volume":"16","author":"Sullivan","year":"1994","journal-title":"Free Radic. Biol. Med"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB8","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1002\/j.1460-2075.1991.tb07761.x","article-title":"Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-\u03baB transcription factor and HIV-1","volume":"10","author":"Schreck","year":"1991","journal-title":"EMBO J."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB9","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S1054-3589(08)60990-4","article-title":"Redox signaling and the control of cell growth and death","volume":"38","author":"Powis","year":"1997","journal-title":"Adv. Pharmacol."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB10","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0165-2478(95)00004-O","article-title":"Effects of N-acetyl-L-cysteine on T-cell apoptosis are not mediated by increased cellular glutathione","volume":"45","author":"Jones","year":"1995","journal-title":"Immunol. Lett."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB11","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0020-7055(74)90024-2","article-title":"The radiolysis of aqueous solutions of cysteine in the presence of oxygen","volume":"6","author":"Al-Thannon","year":"1974","journal-title":"Int. J. Radiat. Phys. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB12","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0020-7055(70)90029-X","article-title":"The radiolysis of oxygenated cysteine solutions of neutral pH: The role of RSSR and superoxide","volume":"2","author":"Barton","year":"1970","journal-title":"Int. J. Radiat. Phys. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB13","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1111\/j.1432-1033.1983.tb07791.x","article-title":"Oxidation of glutathione by the superoxide radical to the disulfide and the sulfonate yielding singlet oxygen","volume":"137","author":"Wefers","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB14","doi-asserted-by":"crossref","first-page":"4718","DOI":"10.1021\/j100165a024","article-title":"The reaction of superoxide radical anion with dithiothreitol: a chain process","volume":"95","author":"Zhang","year":"1991","journal-title":"J. Phys. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB15","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1006\/abbi.1994.1444","article-title":"The reaction of superoxide with reduced glutathione","volume":"314","author":"Winterbourn","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB16","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1039\/p29730001547","article-title":"Kinetics of the reaction of hydrogen peroxide with cysteine and cysteamine","volume":"1973","author":"Barton","year":"1973","journal-title":"J. Chem. Soc. Perkin II"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB17","doi-asserted-by":"crossref","first-page":"4765","DOI":"10.1021\/bi00014a034","article-title":"Reduction of phenoxyl radicals by thioredoxin results in selective oxidation of its SH-groups to disulfides. An antioxidant function of thioredoxin","volume":"34","author":"Goldman","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB18","doi-asserted-by":"crossref","first-page":"119","DOI":"10.3109\/10715769409147509","article-title":"Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation","volume":"20","author":"Scott","year":"1994","journal-title":"Free Radic. Res."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB19","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/0891-5849(89)90066-X","article-title":"The antioxidant action of N-acetylcysteine: Its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid","volume":"6","author":"Aruoma","year":"1989","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB20","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1063\/1.555739","article-title":"Reactivity of HO2\u2022\/O2\u2212 radicals in aqueous solution","volume":"14","author":"Bielski","year":"1985","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB21","unstructured":"Bielski, B. H. J.; Shiue, G. G. Oxygen free radicals and tissue damage. New York: Excerpta Medica; 1979:43\u201356."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB22","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1271\/bbb1961.40.1891","article-title":"Reactivity of thiols with superoxide radicals","volume":"40","author":"Asada","year":"1976","journal-title":"Agric. Biol. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB23","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/abbi.1996.0067","article-title":"Determination of rate constants of the reactions of thiols with superoxide radical by electron paramagnetic resonance: critical remarks on spectrophotometric approaches","volume":"326","author":"Dikalov","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB24","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1006\/bbrc.1996.1492","article-title":"Reevaluation of superoxide scavenging activity of dihydrolipoic acid and its analogues by chemiluminescent method using 2-methyl-6-[p-methoxyphenyl]-3,7-dihydroimidazo-[1,2-a]pyrazine-3-one (MCLA) as a superoxide probe","volume":"227","author":"Matsugo","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB25","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/S0076-6879(94)33056-5","article-title":"Assays for the chlorination activity of myeloperoxidase","volume":"233","author":"Kettle","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB26","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/S0076-6879(94)33021-2","article-title":"Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides","volume":"233","author":"Wolff","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB27","doi-asserted-by":"crossref","first-page":"2151","DOI":"10.1016\/S0021-9258(19)42810-X","article-title":"Generation of superoxide free radical during the oxidation of thiols","volume":"249","author":"Misra","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB28","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1080\/09553009214552111","article-title":"Intramolecular transformation reaction of glutathione thiol radical into a non-sulphur-centered radical: a pulse radiolysis and EPR study","volume":"62","author":"Grierson","year":"1999","journal-title":"Int. J. Radiat. Biol."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB29","doi-asserted-by":"crossref","first-page":"12010","DOI":"10.1021\/ja00105a048","article-title":"Kinetics of one-electron oxidation of thiols and hydrogen abstraction by thiyl radicals from \u03b1-amino C\u2013H bonds","volume":"116","author":"Zhao","year":"1999","journal-title":"J. Amer. Chem. Soc."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB30","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/0167-4838(85)90098-6","article-title":"Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals","volume":"827","author":"Thornalley","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB31","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3109\/10715769109105221","article-title":"Thioctic acid and dihydrolipoic acid are novel antioxidants which interact with reactive oxygen species","volume":"15","author":"Suzuki","year":"1991","journal-title":"Free Radic. Res. Commun."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB32","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1021\/j100233a031","article-title":"Kinetics and mechanism for the oxidation of ascorbic acid\/ascorbate by hydroperoxyl\/superoxide radicals. A pulse radiolysis and stopped flow photolysis study","volume":"87","author":"Cabelli","year":"1983","journal-title":"J. Phys. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB33","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/0304-4165(84)90038-2","article-title":"Superoxide-dependent reduction of nitroxides by thiols","volume":"802","author":"Finkelstein","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB34","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0076-6879(95)51108-3","article-title":"Kinetic factors that control the fate of thiyl radicals in cells","volume":"251","author":"Wardman","year":"1995","journal-title":"Methods Enzymol"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB35","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1006\/abbi.1995.0064","article-title":"Generation of superoxide and tyrosine peroxide as a result of tyrosyl radical scavenging by glutathione","volume":"323","author":"Pichorner","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB36","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/0891-5849(93)90512-S","article-title":"Superoxide as an intracellular radical sink","volume":"14","author":"Winterbourn","year":"1993","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB37","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1096\/fasebj.7.15.8262333","article-title":"Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation","volume":"7","author":"Claiborne","year":"1993","journal-title":"FASEB J."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB38","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0076-6879(94)33047-6","article-title":"Labeling of protein vicinal dithiols: Role of protein-S2 to protein-(SH)2 conversion in metabolic regulation and oxidative stress","volume":"233","author":"Gitler","year":"1994","journal-title":"Methods Enzymol"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB39","doi-asserted-by":"crossref","first-page":"5633","DOI":"10.1021\/bi973035t","article-title":"Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation","volume":"37","author":"Denu","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S0891-5849(99)00051-9_BIB40","doi-asserted-by":"crossref","first-page":"28635","DOI":"10.1074\/jbc.270.48.28635","article-title":"Thioredoxin-linked \u201cthiol peroxidase\u201d from periplasmic space of Escherichia coli","volume":"270","author":"Cha","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB41","doi-asserted-by":"crossref","first-page":"6303","DOI":"10.1074\/jbc.273.11.6303","article-title":"Characterization of a mammalian peroxiredoxin that contains one conserved cysteine","volume":"273","author":"Kang","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0891-5849(99)00051-9_BIB42","series-title":"The chemistry and biochemistry of the sulfhydryl group in amino acids, peptides, and proteins","author":"Friedman","year":"1973"}],"container-title":["Free Radical Biology and Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0891584999000519?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0891584999000519?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,9]],"date-time":"2021-05-09T13:32:23Z","timestamp":1620567143000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0891584999000519"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,8]]},"references-count":42,"journal-issue":{"issue":"3-4","published-print":{"date-parts":[[1999,8]]}},"alternative-id":["S0891584999000519"],"URL":"https:\/\/doi.org\/10.1016\/s0891-5849(99)00051-9","relation":{},"ISSN":["0891-5849"],"issn-type":[{"value":"0891-5849","type":"print"}],"subject":[],"published":{"date-parts":[[1999,8]]}}}