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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2023,1,17]]},"abstract":"<jats:p>\n                    Although hydrogen sulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S) is an endogenous signaling molecule with antioxidant properties, it is also cytotoxic by potently inhibiting cytochrome c oxidase and mitochondrial respiration. Paradoxically, the primary route of H\n                    <jats:sub>2<\/jats:sub>\n                    S detoxification is thought to occur inside the mitochondrial matrix\n                    <jats:italic>via<\/jats:italic>\n                    a series of relatively slow enzymatic reactions that are unlikely to compete with its rapid inhibition of cytochrome c oxidase. Therefore, alternative or complementary cellular mechanisms of H\n                    <jats:sub>2<\/jats:sub>\n                    S detoxification are predicted to exist. Here, superoxide dismutase [Cu-Zn] (SOD1) is shown to be an efficient H\n                    <jats:sub>2<\/jats:sub>\n                    S oxidase that has an essential role in limiting cytotoxicity from endogenous and exogenous sulfide. Decreased SOD1 expression resulted in increased sensitivity to H\n                    <jats:sub>2<\/jats:sub>\n                    S toxicity in yeast and human cells, while increased SOD1 expression enhanced tolerance to H\n                    <jats:sub>2<\/jats:sub>\n                    S. SOD1 rapidly converted H\n                    <jats:sub>2<\/jats:sub>\n                    S to sulfate under conditions of limiting sulfide; however, when sulfide was in molar excess, SOD1 catalyzed the formation of per- and polysulfides, which induce cellular thiol oxidation. Furthermore, in SOD1-deficient cells, elevated levels of reactive oxygen species catalyzed sulfide oxidation to per- and polysulfides. These data reveal that a fundamental function of SOD1 is to regulate H\n                    <jats:sub>2<\/jats:sub>\n                    S and related reactive sulfur species.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2205044120","type":"journal-article","created":{"date-parts":[[2023,1,11]],"date-time":"2023-01-11T13:33:38Z","timestamp":1673444018000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":53,"title":["SOD1 is an essential H\n                    <sub>2<\/sub>\n                    S detoxifying enzyme"],"prefix":"10.1073","volume":"120","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4321-0011","authenticated-orcid":false,"given":"Christopher H.","family":"Switzer","sequence":"first","affiliation":[{"name":"William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London EC1M 6BQ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3094-8543","authenticated-orcid":false,"given":"Shingo","family":"Kasamatsu","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Graduate School of Science, Osaka Metropolitan University, Osaka 599-8531, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hideshi","family":"Ihara","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Graduate School of Science, Osaka Metropolitan University, Osaka 599-8531, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0748-2367","authenticated-orcid":false,"given":"Philip","family":"Eaton","sequence":"additional","affiliation":[{"name":"William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London EC1M 6BQ, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2023,1,11]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(77)90216-X"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.3109\/10408448409029321"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/srep20831"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1161\/HYPERTENSIONAHA.114.04281"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.15252\/emmm.201910695"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1080\/03602530600959607"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2012.5041"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","unstructured":"Q. 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