{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T02:21:03Z","timestamp":1791598863100,"version":"4.3.4"},"reference-count":87,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Nitric Oxide"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.niox.2020.11.004","type":"journal-article","created":{"date-parts":[[2020,11,27]],"date-time":"2020-11-27T20:50:40Z","timestamp":1606510240000},"page":"46-57","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":40,"special_numbering":"C","title":["A comparison of the chemical biology of hydropersulfides (RSSH) with other protective biological antioxidants and nucleophiles"],"prefix":"10.1016","volume":"107","author":[{"given":"Jon M.","family":"Fukuto","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adrian J.","family":"Hobbs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.niox.2020.11.004_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1126\/scisignal.2000464","article-title":"H2S signals through protein S-sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"10.1016\/j.niox.2020.11.004_bib2","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.1321232111","article-title":"Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling","volume":"111","author":"Ida","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.niox.2020.11.004_bib3","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1500968","article-title":"A\u00a0novel persulfide detection method reveals protein persulfide- and polysulfide-reducing function of thioredoxin and glutathione systems","volume":"2","author":"Doka","year":"2016","journal-title":"Sci. Adv."},{"issue":"10","key":"10.1016\/j.niox.2020.11.004_bib4","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1089\/ars.2017.7081","article-title":"Chemical biology of hydropersulfides and related species: possible roles in cellular protection and redox signaling","volume":"27","author":"Alvarez","year":"2017","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2020.11.004_bib5","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1002\/1873-3468.13090","article-title":"Biological hydropersulfides and related polysulfides \u2013 a new concept and perspective in redox biology","volume":"592","author":"Fukuto","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.niox.2020.11.004_bib6","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/acs.chemrev.7b00205","article-title":"Chemic al biology of H2S signaling through presulfidation","volume":"118","author":"Filipovic","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.niox.2020.11.004_bib7","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1089\/ars.2012.5041","article-title":"Polysulfides link H2S to protein thiol oxidation","volume":"19","author":"Greiner","year":"2013","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2020.11.004_bib8","doi-asserted-by":"crossref","first-page":"6324","DOI":"10.1002\/anie.201803087","article-title":"A\u00a0persulfide donor responsive to reactive oxygen species: insights into reactivity and therapeutic potential","volume":"57","author":"Powell","year":"2018","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.niox.2020.11.004_bib9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chembiol.2018.01.011","article-title":"N-Acetyl cysteine functions as a fast-acting antioxidant by triggering intracellular H2S and sulfane sulfur production","volume":"25","author":"Ezerina","year":"2018","journal-title":"Cell. Chem. Biol."},{"key":"10.1016\/j.niox.2020.11.004_bib10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chembiol.2019.02.003","article-title":"Enhanced cellular polysulfides negatively regulate TLR4 signaling and mitigate lethal endotoxin shock","volume":"26","author":"Zhang","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.niox.2020.11.004_bib11","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1111\/bph.14372","article-title":"The reaction of hydrogen sulfide with disulfides: formation of a stable trisulfide and implications to biological systems","volume":"176","author":"Bianco","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.niox.2020.11.004_bib12","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1021\/acs.chemrestox.9b00494","article-title":"Cysteine trisulfide protects E. coli from electrophile-induced death through the generation of cysteine hydropersulfide","volume":"33","author":"Henderson","year":"2020","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.niox.2020.11.004_bib13","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1146\/annurev.nu.06.070186.001143","article-title":"Metabolism of sulfur-containing amino acids","volume":"6","author":"Stipanuk","year":"1986","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.niox.2020.11.004_bib14","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1021\/jacs.5b10494","article-title":"Biosynthesis and reactivity of cysteine persulfides in signaling","volume":"138","author":"Yadav","year":"2016","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.niox.2020.11.004_bib15","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.cbpa.2017.02.021","article-title":"Catalytic promiscuity and heme-dependent redox regulation of H2S synthesis","volume":"37","author":"Banerjee","year":"2017","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.niox.2020.11.004_bib16","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1021\/tx2005234","article-title":"Small molecule signaling agents: the integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide, and their derived species","volume":"25","author":"Fukuto","year":"2012","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.niox.2020.11.004_bib17","doi-asserted-by":"crossref","first-page":"R1479","DOI":"10.1152\/ajpregu.90566.2008","article-title":"Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values","volume":"295","author":"Furne","year":"2008","journal-title":"Am. J. Physiol. Integr. Comp. Physiol."},{"key":"10.1016\/j.niox.2020.11.004_bib18","doi-asserted-by":"crossref","first-page":"29808","DOI":"10.1038\/srep29808","article-title":"Quantitative persulfide site identification (qPerS-SID) reveals protein targets of H2S releasing donors in mammalian cells","volume":"6","author":"Longen","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.niox.2020.11.004_bib19","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1111\/bph.14394","article-title":"Speciation of reactive sulfur species and their reactions with alkylating agents: do we have any clue about what is present inside the cell?","volume":"176","author":"Bogdandi","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.niox.2020.11.004_bib20","doi-asserted-by":"crossref","first-page":"26866","DOI":"10.1074\/jbc.M115.672816","article-title":"Reaction of hydropgen sulfide with disulfide and sulfenic acid to form the strongly nucleophilic persulfide","volume":"290","author":"Cuevasanta","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib21","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0076-6879(87)43009-7","article-title":"Sulfane sulfur","volume":"143","author":"Wood","year":"1987","journal-title":"Methods Enzymol."},{"issue":"2","key":"10.1016\/j.niox.2020.11.004_bib22","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20150147","article-title":"S-sulfhydration as a cellular redox regulation","volume":"36","author":"Iciek","year":"2016","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.niox.2020.11.004_bib23","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.abb.2016.09.018","article-title":"Biological chemistry of hydrogen sulfide and persulfides","volume":"617","author":"Cuevasanta","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib24","doi-asserted-by":"crossref","first-page":"1827","DOI":"10.1021\/ja00984a014","article-title":"Application of the principle of hard and soft acids and bases to organic chemistry","volume":"89","author":"Pearson","year":"1967","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.niox.2020.11.004_bib25","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1021\/ja01004a002","article-title":"Chemical reactivity and the concept of charge- and frontier-controlled reactions","volume":"90","author":"Klopman","year":"1968","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.niox.2020.11.004_bib26","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1021\/cr50028a003","article-title":"The scission of the sulfur-sulfur bond","volume":"59","author":"Parker","year":"1959","journal-title":"Chem. Rev."},{"key":"10.1016\/j.niox.2020.11.004_bib27","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.abb.2015.10.016","article-title":"The chemical biology of hydropersulfides (RSSH): chemical stability, reactivity and redox roles","volume":"588","author":"Saund","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib28","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0076-6879(95)51110-5","article-title":"Perthiols as antioxidants: radical-scavenging and prooxidative mechanisms","volume":"251","author":"Everett","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.niox.2020.11.004_bib29","doi-asserted-by":"crossref","first-page":"7290","DOI":"10.1021\/jo801215z","article-title":"Nucleophilicity and leaving group ability in frontside and backside SN2 reactions","volume":"73","author":"Bento","year":"2008","journal-title":"J.\u00a0Org. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib30","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1021\/ja00860a005","article-title":"The factors determining nucleophilic reactivities","volume":"84","author":"Edwards","year":"1961","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.niox.2020.11.004_bib31","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1021\/cr60311a003","article-title":"Thermochemistry and kinetics of sulfur-containing molecules and radicals","volume":"78","author":"Benson","year":"1978","journal-title":"Chem. Rev."},{"key":"10.1016\/j.niox.2020.11.004_bib32","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.freeradbiomed.2016.09.020","article-title":"The chemical biology of the persulfide (RSSH)\/perthiyl (RSS\u00b7) redox couple and possible role in biological redox signaling","volume":"101","author":"Bianco","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib33","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.1021\/jacs.7b02571","article-title":"Hydropersulfides: H-atom transfer agents par excellence","volume":"139","author":"Chauvin","year":"2017","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.niox.2020.11.004_bib34","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.abb.2016.09.012","article-title":"Signaling by sulfur-containing molecules. Quantitative aspects","volume":"617","author":"Koppenol","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib35","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.abb.2011.09.015","article-title":"The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology","volume":"516","author":"Francoleon","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib36","doi-asserted-by":"crossref","first-page":"108391","DOI":"10.1016\/j.abb.2020.108391","article-title":"The reactions of hydropersulfides (RSSH) with myoglobin","volume":"687","author":"Alvarez","year":"2020","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib37","doi-asserted-by":"crossref","first-page":"C537","DOI":"10.1152\/ajpcell.00101.2016","article-title":"4-Hydroxy-2-nonenal: a critical target in oxidative stress?","volume":"311","author":"Breitzig","year":"2016","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.niox.2020.11.004_bib38","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.freeradbiomed.2016.05.013","article-title":"The chemical biology of protein hydropersulfides: studies of a possible protective function of biological hydropersulfide generation","volume":"97","author":"Millikin","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib39","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1113\/expphysiol.1997.sp004024","article-title":"Oxidative stress: oxidants and antioxidants","volume":"82","author":"Sies","year":"1997","journal-title":"Exp. Physiol."},{"key":"10.1016\/j.niox.2020.11.004_bib40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mam.2008.08.006","article-title":"Glutathione: overview of its protective roles, measurement, and biosynthesis","volume":"30","author":"Forman","year":"2009","journal-title":"Mol. Aspect. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib41","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.coph.2007.06.003","article-title":"Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress","volume":"7","author":"Gallogly","year":"2007","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.niox.2020.11.004_bib42","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fonc.2014.00359","article-title":"Ascorbate as a co-factor for Fe- and 2-oxoglutarate dependent dioxygenase: physiological activity in tumor growth and progression","volume":"4","author":"Kuiper","year":"2014","journal-title":"Front. Oncol."},{"key":"10.1016\/j.niox.2020.11.004_bib43","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1042\/bj1980125","article-title":"Hydroxyl radical production in body fluids","volume":"198","author":"Winterbourn","year":"1981","journal-title":"Biochem. J."},{"issue":"8","key":"10.1016\/j.niox.2020.11.004_bib44","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1001\/jama.297.8.842","article-title":"Mortality in randomized trials of antioxidant supplements for primary and secondary prevention","volume":"297","author":"Bjelakovic","year":"2007","journal-title":"J.\u00a0Am. Med. Assoc."},{"key":"10.1016\/j.niox.2020.11.004_bib45","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1104\/pp.104.2.617","article-title":"Inhibition of apoplastic and symplastic peroxidase activity from Norway Spruceby the photooxidant hydroxymethyl hydroperoxide","volume":"104","author":"Polle","year":"1994","journal-title":"Plant Physiol."},{"key":"10.1016\/j.niox.2020.11.004_bib46","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.redox.2017.03.020","article-title":"Cysteine persulfides and polysulfides produced by exchange reactions with H2S protect SH-SY5Y cells from methylglyoxal-induced toxicity through Nrf2 activation","volume":"12","author":"Koike","year":"2017","journal-title":"Redox Biol."},{"key":"10.1016\/j.niox.2020.11.004_bib47","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1152\/physrev.00023.2017","article-title":"The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis","volume":"98","author":"Yamamoto","year":"2018","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.niox.2020.11.004_bib48","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.1089\/ars.2012.4645","article-title":"Hydrogen sulfide protects against cellular senescence via S-sulfhydration of Keap1 and activation of Nrf2","volume":"18","author":"Yang","year":"2013","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2020.11.004_bib49","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1016\/j.freeradbiomed.2009.09.018","article-title":"Making and working with hydrogen sulfide, the chemistry and generation of hydrogen sulfide in\u00a0vitro and its measurement in\u00a0vivo: a review","volume":"47","author":"Hughes","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib50","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1146\/annurev.bi.52.070183.003431","article-title":"Glutathione","volume":"52","author":"Meister","year":"1983","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.niox.2020.11.004_bib51","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1146\/annurev.pharmtox.45.120403.095857","article-title":"Glutathione transferases","volume":"45","author":"Hayes","year":"2005","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.niox.2020.11.004_bib52","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1016\/j.bbagen.2008.06.003","article-title":"Glutaredoxin systems","volume":"1780","author":"Lillig","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.niox.2020.11.004_bib53","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1016\/j.bbagen.2012.11.020","article-title":"Glutahione peroxidases","volume":"1830","author":"Brigelius-Flohe","year":"2012","journal-title":"Biochim. Biopys. Acta"},{"key":"10.1016\/j.niox.2020.11.004_bib54","doi-asserted-by":"crossref","first-page":"3217","DOI":"10.1016\/j.bbagen.2012.09.018","article-title":"Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes","volume":"1830","author":"Deponte","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.niox.2020.11.004_bib55","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s00726-010-0602-7","article-title":"Why do proteins use selenocysteine instead of cysteine?","volume":"42","author":"Nauser","year":"2012","journal-title":"Amino Acids"},{"key":"10.1016\/j.niox.2020.11.004_bib56","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1089\/ars.2020.8079","article-title":"Predicting the possible physiological\/biological utility of the hydropersulfide functional group based on its chemistry: similarities between hydropersulfides and selenols","volume":"33","author":"Fukuto","year":"2020","journal-title":"Antiox. Redox Sign."},{"key":"10.1016\/j.niox.2020.11.004_bib57","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1089\/ars.2007.1716","article-title":"Molecular mechanisms and potential clinical significance of S-glutathionylation","volume":"10","author":"Dalle-Donne","year":"2008","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2020.11.004_bib58","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.freeradbiomed.2018.03.038","article-title":"An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation","volume":"120","author":"Zhang","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib59","first-page":"28983","article-title":"Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, NO release, and biological activity","volume":"274","author":"Woltz","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib60","doi-asserted-by":"crossref","first-page":"3165","DOI":"10.1016\/j.bbagen.2013.02.009","article-title":"Protein glutathionylation in health and disease","volume":"1830","author":"Ghezzi","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.niox.2020.11.004_bib61","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.exer.2004.02.001","article-title":"Protein S-glutathioylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone","volume":"78","author":"Hoppe","year":"2004","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.niox.2020.11.004_bib62","doi-asserted-by":"crossref","first-page":"4170","DOI":"10.1073\/pnas.93.9.4170","article-title":"The phosphatase activity of carbonicanhydrase III is reversibly regulated by glutathionylation","volume":"93","author":"Cabiscol","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.niox.2020.11.004_bib63","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.toxlet.2010.08.011","article-title":"PYDDT, a novel phase 2 enzymes inducer, activates Keap1-Nrf2 pathway via depleting the cellular level of glutathione","volume":"199","author":"Zhang","year":"2010","journal-title":"Toxicol. Lett."},{"key":"10.1016\/j.niox.2020.11.004_bib64","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1002\/1873-3468.12177","article-title":"S-Glutathionylation of Keap1: a new role for glutathione S-transferase pi in neuronal protection","volume":"590","author":"Carvalho","year":"2016","journal-title":"FEBS Lett."},{"key":"10.1016\/j.niox.2020.11.004_bib65","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1038\/ncomms2623","article-title":"Sulfhydration mediates neuroprotective actions of parkin","volume":"4","author":"Vandiver","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.niox.2020.11.004_bib66","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0003-9861(91)90452-O","article-title":"Nitric oxide as an antioxidant","volume":"289","author":"Kanner","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib67","doi-asserted-by":"crossref","first-page":"9813","DOI":"10.1073\/pnas.90.21.9813","article-title":"Nitric oxide protects against cellular damage and cytotoxicity from reactive oxygen species","volume":"90","author":"Wink","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.niox.2020.11.004_bib68","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0014-5793(95)00786-9","article-title":"Action of nitric oxide as an antioxidant against oxidation of soybean phosphatidylcholine liposomal membranes","volume":"370","author":"Hayashi","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.niox.2020.11.004_bib69","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1016\/S0022-2275(20)41494-4","article-title":"Inhibition of macrophage-dependent low density lipoprotein oxidation by nitric oxide donors","volume":"36","author":"Hogg","year":"1995","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.niox.2020.11.004_bib70","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1006\/abbi.1995.9935","article-title":"Nitric oxide inhibition of lipoxygenase-dependent liposome and low-density lipoprotein oxidation: termination of radical chain propagating reactions and formation of nitrogen-containing oxidized lipid derivatives","volume":"324","author":"Rubbo","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2020.11.004_bib71","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1023\/A:1020150124721","article-title":"Nitric oxide: a unique endogenous signaling molecule in vascular biology","volume":"19","author":"Ignarro","year":"1999","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.niox.2020.11.004_bib72","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/S0165-6147(97)90687-8","article-title":"Soluble guanylate cyclase: the forgotten sibling","volume":"18","author":"Hobbs","year":"1997","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.niox.2020.11.004_bib73","doi-asserted-by":"crossref","DOI":"10.1002\/prp2.261","article-title":"Soluble guanylate cyclase redox state under oxidative stress conditions in isolated monkey coronary arteries","author":"Tawa","year":"2016","journal-title":"Pharma Res. Per."},{"key":"10.1016\/j.niox.2020.11.004_bib74","doi-asserted-by":"crossref","first-page":"256","DOI":"10.4161\/cc.4.2.1407","article-title":"Inflammatory hypoxia, role of hypoxia-inducible factor","volume":"4","author":"Karhausen","year":"2005","journal-title":"Cell Cycle"},{"key":"10.1016\/j.niox.2020.11.004_bib75","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.bbadis.2015.10.017","article-title":"Acidosis differently modulates the inflammatory program in monocytes and macrophages","volume":"1862","author":"Riemann","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.niox.2020.11.004_bib76","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/S0891-5849(99)00051-9","article-title":"Reactivity of biologically important compounds with superoxide and hydrogen peroxide","volume":"27","author":"Winterbourn","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib77","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1021\/cr300163e","article-title":"Cysteine-mediated redox signaling: chemistry, biology, and tools","volume":"113","author":"Paulson","year":"2013","journal-title":"Chem. Rev."},{"key":"10.1016\/j.niox.2020.11.004_bib78","doi-asserted-by":"crossref","first-page":"2508","DOI":"10.1021\/jo00214a020","article-title":"Mechanism of the oxidation of o-nitro- and o-benzylbenzeneselenenic acids by peracids, hydroperxoides, and hydrogen peroxide","volume":"50","author":"Kice","year":"1985","journal-title":"J.\u00a0Org. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib79","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/9780470171837.ch3","article-title":"Nucleophilic displacement on peroxide oxygen and related reactions","volume":"4","author":"Behrman","year":"1967","journal-title":"Prog. Phys. Org. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib80","doi-asserted-by":"crossref","first-page":"18048","DOI":"10.1074\/jbc.M111.232355","article-title":"Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide","volume":"286","author":"Nagy","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.niox.2020.11.004_bib81","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1021\/tx960072x","article-title":"Structure, catalytic mechanism, and evolution of r glutathione transferases","volume":"10","author":"Armstrong","year":"1997","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.niox.2020.11.004_bib82","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.jmb.2010.07.022","article-title":"Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization","volume":"402","author":"Hall","year":"2010","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.niox.2020.11.004_bib83","first-page":"1","article-title":"The alpha effect. A review","author":"Fina","year":"1976","journal-title":"Int. J. Chem. Kinet. V"},{"key":"10.1016\/j.niox.2020.11.004_bib84","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.freeradbiomed.2015.09.007","article-title":"Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is inactivated by S-sulfuration, in\u00a0vitro","volume":"89","author":"Jarosz","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.niox.2020.11.004_bib85","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.1016\/j.bbagen.2009.04.007","article-title":"Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme","volume":"1790","author":"Toppo","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"issue":"1177","key":"10.1016\/j.niox.2020.11.004_bib86","first-page":"1","article-title":"Cysteinyl-tRNA synthase governs cysteine polysulfidation and mitochondrial bioenergetics","volume":"8","author":"Akaike","year":"2017","journal-title":"Nature Comm."},{"key":"10.1016\/j.niox.2020.11.004_bib87","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.freeradbiomed.2014.09.007","article-title":"The redox chemistry and chemical biology of H2S, hydropersulfides and derived species: Implications of their possible biological activity and utility,","volume":"77","author":"Ono","year":"2014","journal-title":"Free Radic. Biol. Med."}],"container-title":["Nitric Oxide"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1089860320302020?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1089860320302020?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T18:06:16Z","timestamp":1761069976000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1089860320302020"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":87,"alternative-id":["S1089860320302020"],"URL":"https:\/\/doi.org\/10.1016\/j.niox.2020.11.004","relation":{},"ISSN":["1089-8603"],"issn-type":[{"value":"1089-8603","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A comparison of the chemical biology of hydropersulfides (RSSH) with other protective biological antioxidants and nucleophiles","name":"articletitle","label":"Article Title"},{"value":"Nitric Oxide","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.niox.2020.11.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}