{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T00:21:37Z","timestamp":1789431697118,"version":"build-2803163510"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,10,15]],"date-time":"2021-10-15T00:00:00Z","timestamp":1634256000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["91951202"],"award-info":[{"award-number":["91951202"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2018YFA0901200"],"award-info":[{"award-number":["2018YFA0901200"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009108","name":"Shandong University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009108","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100017133","name":"National Key Project for Synthetic Biology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100017133","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2021,11]]},"DOI":"10.1016\/j.redox.2021.102169","type":"journal-article","created":{"date-parts":[[2021,10,19]],"date-time":"2021-10-19T06:53:06Z","timestamp":1634626386000},"page":"102169","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"special_numbering":"C","title":["Sulfide-quinone oxidoreductase is required for cysteine synthesis and indispensable to mitochondrial health"],"prefix":"10.1016","volume":"47","author":[{"given":"Xi","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuping","family":"Xin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhigang","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9950-1910","authenticated-orcid":false,"given":"Yongzhen","family":"Xia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5770-9016","authenticated-orcid":false,"given":"Luying","family":"Xun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0483-5318","authenticated-orcid":false,"given":"Huaiwei","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.redox.2021.102169_bib1","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0005-2728(96)00077-1","article-title":"Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications","volume":"1276","author":"Papa","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.redox.2021.102169_bib2","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/s41556-018-0124-1","article-title":"The multifaceted contributions of mitochondria to cellular metabolism","volume":"20","author":"Spinelli","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.redox.2021.102169_bib3","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/s41556-018-0176-2","article-title":"Mechanisms of mitophagy in cellular homeostasis, physiology and pathology","volume":"20","author":"Palikaras","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.redox.2021.102169_bib4","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/nature12985","article-title":"Mitochondrial form and function","volume":"505","author":"Friedman","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.redox.2021.102169_bib5","doi-asserted-by":"crossref","first-page":"42","DOI":"10.2741\/4375","article-title":"Mitochondrial DNA damage induced autophagy, cell death, and disease","volume":"21","author":"Van Houten","year":"2016","journal-title":"Front. Biosci. - Landmark."},{"key":"10.1016\/j.redox.2021.102169_bib6","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.trecan.2020.04.009","article-title":"Mitochondrial stress response and cancer","volume":"6","author":"O'Malley","year":"2020","journal-title":"Trends in Cancer"},{"key":"10.1016\/j.redox.2021.102169_bib7","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1111\/bph.14330","article-title":"Inorganic hydrogen polysulfides: chemistry, chemical biology and detection","volume":"176","author":"Liu","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.redox.2021.102169_bib8","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.redox.2021.102169_bib9","first-page":"533","article-title":"Sulfane sulfur - new findings on an old topic","volume":"66","author":"Iciek","year":"2019","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.redox.2021.102169_bib10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cbpa.2018.08.012","article-title":"Reactive sulfur species (RSS): persulfides, polysulfides, potential, and problems","volume":"49","author":"Lau","year":"2019","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.redox.2021.102169_bib11","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3164\/jcbn.20-13","article-title":"Antioxidative and anti-inflammatory actions of reactive cysteine persulfides","volume":"68","author":"Zhang","year":"2021","journal-title":"J. Clin. Biochem. Nutr."},{"key":"10.1016\/j.redox.2021.102169_bib12","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nchembio.1834","article-title":"Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways","volume":"11","author":"Mishanina","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.redox.2021.102169_bib13","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1038\/ismej.2017.125","article-title":"Sulfide production and oxidation by heterotrophic bacteria under aerobic conditions","volume":"11","author":"Xia","year":"2017","journal-title":"ISME J."},{"key":"10.1016\/j.redox.2021.102169_bib14","first-page":"1699","article-title":"Sulfide, the first inorganic substrate for human cells","volume":"21","author":"Goubern","year":"2007","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"10.1016\/j.redox.2021.102169_bib15","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1007\/s00360-012-0654-y","article-title":"Mitochondrial adaptations to utilize hydrogen sulfide for energy and signaling","volume":"182","author":"Olson","year":"2012","journal-title":"J. Comp. Physiol. B Biochem. Syst. Environ. Physiol."},{"key":"10.1016\/j.redox.2021.102169_bib16","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1089\/ars.2011.4310","article-title":"High turnover rates for hydrogen sulfide allow for rapid regulation of its tissue concentrations","volume":"17","author":"Vitvitsky","year":"2012","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2021.102169_bib17","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1086\/381653","article-title":"Ethylmalonic encephalopathy is caused by mutations in ETHE1, a gene encoding a mitochondrial matrix protein","volume":"74","author":"Tiranti","year":"2004","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.redox.2021.102169_bib18","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-017-01311-y","article-title":"Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics","volume":"8","author":"Akaike","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.redox.2021.102169_bib19","doi-asserted-by":"crossref","first-page":"379\u2014391","DOI":"10.1089\/ars.2010.3678","article-title":"Mitochondria and sulfide: a very old story of poisoning, feeding, and signaling?","volume":"15","author":"Bouillaud","year":"2011","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2021.102169_bib20","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1534\/genetics.115.181503","article-title":"An ancient yeast for young geneticists: a primer on the Schizosaccharomyces pombe model system","volume":"201","author":"Hoffman","year":"2015","journal-title":"Genetics"},{"key":"10.1016\/j.redox.2021.102169_bib21","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1089\/dna.1995.14.359","article-title":"Schizosaccharomyces pombe: a model for molecular studies of eukaryotic genes","volume":"14","author":"Zhao","year":"1995","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.redox.2021.102169_bib22","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1038\/nature724","article-title":"The genome sequence of Schizosaccharomyces pombe","volume":"415","author":"Wood","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.redox.2021.102169_bib23","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1111\/mmi.12835","article-title":"The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus","volume":"94","author":"Luebke","year":"2014","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.redox.2021.102169_bib24","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1128\/AEM.03281-13","article-title":"Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria","volume":"80","author":"Liu","year":"2014","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.redox.2021.102169_bib25","doi-asserted-by":"crossref","first-page":"6633","DOI":"10.1021\/es049514e","article-title":"Equilibrium distribution of polysulfide ions in aqueous solutions at 25 degrees C: a new approach for the study of polysulfides' equilibria","volume":"38","author":"Kamyshny","year":"2004","journal-title":"Environ. Sci. Technol."},{"key":"10.1016\/j.redox.2021.102169_bib26","doi-asserted-by":"crossref","first-page":"5123","DOI":"10.1111\/1462-2920.13511","article-title":"Recombinant Escherichia coli with sulfide:quinone oxidoreductase and persulfide dioxygenase rapidly oxidises sulfide to sulfite and thiosulfate via a new pathway","volume":"18","author":"Xin","year":"2016","journal-title":"Environ. Microbiol."},{"key":"10.1016\/j.redox.2021.102169_bib27","doi-asserted-by":"crossref","DOI":"10.1021\/acs.analchem.9b02875","article-title":"Sensitive method for reliable quantification of sulfane sulfur in biological samples","volume":"91","author":"Ran","year":"2019","journal-title":"Anal. Chem."},{"key":"10.1016\/j.redox.2021.102169_bib28","doi-asserted-by":"crossref","first-page":"4955","DOI":"10.1016\/S0021-9258(18)99657-2","article-title":"The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium","volume":"241","author":"Kredich","year":"1966","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2021.102169_bib29","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.niox.2013.07.002","article-title":"Hydrogen sulfide chemical biology: pathophysiological roles and detection","volume":"35","author":"Kolluru","year":"2013","journal-title":"Nitric Oxide Biol. Chem."},{"key":"10.1016\/j.redox.2021.102169_bib30","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1083\/jcb.139.3.729","article-title":"A yeast mutant showing diagnostic markers of early and late apoptosis","volume":"139","author":"Madeo","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.redox.2021.102169_bib31","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1083\/jcb.200310014","article-title":"Chronological aging leads to apoptosis in yeast","volume":"164","author":"Herker","year":"2004","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.redox.2021.102169_bib32","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/S0076-6879(97)83026-1","article-title":"Flow cytometric analysis of DNA content in budding yeast","volume":"283","author":"Haase","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.redox.2021.102169_bib33","article-title":"Signalling by hydrogen sulfide and polysulfides via protein S-sulfuration","author":"Kimura","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.redox.2021.102169_bib34","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1021\/acschembio.8b00230","article-title":"Hydrogen sulfide sensing through reactive sulfur species (RSS) and nitroxyl (HNO) in Enterococcus faecalis","volume":"13","author":"Shen","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.redox.2021.102169_bib35","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/acs.chemrev.7b00205","article-title":"Chemical biology of H(2)S signaling through persulfidation","volume":"118","author":"Filipovic","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.redox.2021.102169_bib36","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.redox.2021.102169_bib37","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. Unit. States Am."},{"key":"10.1016\/j.redox.2021.102169_bib38","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/S1369-5266(00)00063-7","article-title":"Regulation of sulfate transport and synthesis of sulfur-containing amino acids","volume":"3","author":"Saito","year":"2000","journal-title":"Curr. Opin. Plant Biol."},{"key":"10.1016\/j.redox.2021.102169_bib39","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1038\/s41416-020-01156-1","article-title":"Cysteine metabolic circuitries: druggable targets in cancer","volume":"124","author":"Bonif\u00e1cio","year":"2021","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.redox.2021.102169_bib40","doi-asserted-by":"crossref","first-page":"8203","DOI":"10.1007\/s00253-018-9246-4","article-title":"Current understanding of sulfur assimilation metabolism to biosynthesize L-cysteine and recent progress of its fermentative overproduction in microorganisms","volume":"102","author":"Kawano","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.redox.2021.102169_bib41","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1128\/jb.158.3.1122-1127.1984","article-title":"Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium","volume":"158","author":"Nakamura","year":"1984","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.redox.2021.102169_bib42","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/BF00407763","article-title":"O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue","volume":"134","author":"Hensel","year":"1983","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.redox.2021.102169_bib43","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1007\/s00216-020-03086-6","article-title":"Mitochondrion-targeting near-infrared fluorescent probe for detecting intracellular nanomolar level hydrogen sulfide with high recognition rate","volume":"413","author":"Zhang","year":"2021","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.redox.2021.102169_bib44","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1089\/ars.2014.5869","article-title":"Signaling molecules: hydrogen sulfide and polysulfide","volume":"22","author":"Kimura","year":"2015","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2021.102169_bib45","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.freeradbiomed.2014.09.007","article-title":"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."},{"key":"10.1016\/j.redox.2021.102169_bib46","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1039\/C5MB00216H","article-title":"Persulfides: current knowledge and challenges in chemistry and chemical biology","volume":"11","author":"Park","year":"2015","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.redox.2021.102169_bib47","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1038\/nchembio.2397","article-title":"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis","volume":"13","author":"Bastard","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.redox.2021.102169_bib48","doi-asserted-by":"crossref","first-page":"3893","DOI":"10.1021\/acs.analchem.8b04634","article-title":"Developing polysulfide-sensitive GFPs for real-time analysis of polysulfides in live cells and subcellular organelles","volume":"91","author":"Hu","year":"2019","journal-title":"Anal. Chem."}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231721003293?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231721003293?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T06:19:48Z","timestamp":1761977988000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231721003293"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,11]]},"references-count":48,"alternative-id":["S2213231721003293"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2021.102169","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2021,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Sulfide-quinone oxidoreductase is required for cysteine synthesis and indispensable to mitochondrial health","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2021.102169","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"102169"}}