{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T06:59:18Z","timestamp":1792652358493,"version":"4.5.0"},"reference-count":55,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,11,17]],"date-time":"2021-11-17T00:00:00Z","timestamp":1637107200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM130183"],"award-info":[{"award-number":["GM130183"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["R01CA244931"],"award-info":[{"award-number":["R01CA244931"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["HL152605"],"award-info":[{"award-number":["HL152605"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["CA203542"],"award-info":[{"award-number":["CA203542"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["HL149633"],"award-info":[{"award-number":["HL149633"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000968","name":"American Heart Association","doi-asserted-by":"publisher","award":["826245"],"award-info":[{"award-number":["826245"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2022,1]]},"DOI":"10.1016\/j.jbc.2021.101435","type":"journal-article","created":{"date-parts":[[2021,11,19]],"date-time":"2021-11-19T10:31:15Z","timestamp":1637317875000},"page":"101435","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":79,"title":["A redox cycle with complex II prioritizes sulfide quinone oxidoreductase-dependent H2S oxidation"],"prefix":"10.1016","volume":"298","author":[{"given":"Roshan","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron P.","family":"Landry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arkajit","family":"Guha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Vitvitsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3616-5387","authenticated-orcid":false,"given":"Ho Joon","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3484-0265","authenticated-orcid":false,"given":"Keisuke","family":"Seike","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavan","family":"Reddy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Costas A.","family":"Lyssiotis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruma","family":"Banerjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2021.101435_bib1","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1523\/JNEUROSCI.16-03-01066.1996","article-title":"The possible role of hydrogen sulfide as an endogenous neuromodulator","volume":"16","author":"Abe","year":"1996","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.jbc.2021.101435_bib2","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1080\/10409238.2021.1893641","article-title":"Regulation of the redox metabolome and thiol proteome by hydrogen sulfide","volume":"56","author":"Kumar","year":"2021","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101435_bib3","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/acs.chemrev.7b00205","article-title":"Chemical biology of H2S signaling through persulfidation","volume":"118","author":"Filipovic","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2021.101435_bib4","doi-asserted-by":"crossref","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.jbc.2021.101435_bib5","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.10067","article-title":"Quantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response","volume":"4","author":"Gao","year":"2015","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2021.101435_bib6","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1500968","article-title":"A\u00a0novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems","volume":"2","author":"Doka","year":"2016","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2021.101435_bib7","doi-asserted-by":"crossref","first-page":"30901","DOI":"10.1074\/jbc.M114.602664","article-title":"Organization of the human mitochondrial sulfide oxidation pathway","volume":"289","author":"Libiad","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib8","doi-asserted-by":"crossref","first-page":"8310","DOI":"10.1074\/jbc.M115.639831","article-title":"Sulfide oxidation by a noncanonical pathway in red blood cells generates thiosulfate and polysulfides","volume":"290","author":"Vitvitsky","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib9","doi-asserted-by":"crossref","first-page":"8476","DOI":"10.1021\/jacs.6b03456","article-title":"Hydrogen sulfide oxidation by myoglobin","volume":"138","author":"Bostelaar","year":"2016","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2021.101435_bib10","doi-asserted-by":"crossref","first-page":"6512","DOI":"10.1074\/jbc.M116.770370","article-title":"A\u00a0distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin","volume":"292","author":"Ruetz","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib11","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1139\/o82-076","article-title":"Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system","volume":"60","author":"Nicholls","year":"1982","journal-title":"Can. J. Biochem."},{"key":"10.1016\/j.jbc.2021.101435_bib12","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1002\/cbic.202000661","article-title":"Hydrogen sulfide oxidation by sulfide quinone oxidoreductase","volume":"22","author":"Landry","year":"2021","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2021.101435_bib13","doi-asserted-by":"crossref","first-page":"1699","DOI":"10.1096\/fj.06-7407com","article-title":"Sulfide, the first inorganic substrate for human cells","volume":"21","author":"Goubern","year":"2007","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2021.101435_bib14","doi-asserted-by":"crossref","first-page":"3352","DOI":"10.1111\/j.1742-4658.2008.06482.x","article-title":"Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria","volume":"275","author":"Hildebrandt","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2021.101435_bib15","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.jbc.2021.101435_bib16","doi-asserted-by":"crossref","first-page":"12077","DOI":"10.1074\/jbc.RA119.009442","article-title":"Hydrogen sulfide perturbs mitochondrial bioenergetics and triggers metabolic reprogramming in colon cells","volume":"294","author":"Libiad","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib17","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1016\/j.bbabio.2010.04.004","article-title":"Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes","volume":"1797","author":"Lagoutte","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2021.101435_bib18","doi-asserted-by":"crossref","first-page":"525","DOI":"10.3389\/fphys.2017.00525","article-title":"The role of sulfide oxidation impairment in the pathogenesis of primary CoQ deficiency","volume":"8","author":"Quinzii","year":"2017","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jbc.2021.101435_bib19","doi-asserted-by":"crossref","first-page":"100736","DOI":"10.1016\/j.jbc.2021.100736","article-title":"The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis","volume":"296","author":"Vitvitsky","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib20","doi-asserted-by":"crossref","first-page":"100950","DOI":"10.1016\/j.jbc.2021.100950","article-title":"Hydrogen sulfide stimulates lipid biogenesis from glutamine that is dependent on the mitochondrial NAD(P)H pool","volume":"297","author":"Carballal","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib21","doi-asserted-by":"crossref","first-page":"3108","DOI":"10.1038\/s41467-021-23363-x","article-title":"Sulfide catabolism ameliorates hypoxic brain injury","volume":"12","author":"Marutani","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101435_bib22","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aaz5752","article-title":"SQR mediates therapeutic effects of H2S by targeting mitochondrial electron transport to induce mitochondrial uncoupling","volume":"6","author":"Jia","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2021.101435_bib23","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nature13909","article-title":"Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS","volume":"515","author":"Chouchani","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101435_bib24","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41420-017-0010-9","article-title":"Glucose-6-phosphate dehydrogenase is critical for suppression of cardiac hypertrophy by H2S","volume":"4","author":"Chhabra","year":"2018","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.jbc.2021.101435_bib25","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1111\/j.1365-2672.1992.tb05187.x","article-title":"Comparison of fermentation reactions in different regions of the human colon","volume":"72","author":"Macfarlane","year":"1992","journal-title":"J.\u00a0Appl. Bacteriol."},{"key":"10.1016\/j.jbc.2021.101435_bib26","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1177\/153537020322800413","article-title":"Gastrointestinal and microbial responses to sulfate-supplemented drinking water in mice","volume":"228","author":"Deplancke","year":"2003","journal-title":"Exp. Biol. Med. (Maywood)"},{"key":"10.1016\/j.jbc.2021.101435_bib27","doi-asserted-by":"crossref","first-page":"11641","DOI":"10.1074\/jbc.M117.788547","article-title":"H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase","volume":"292","author":"Landry","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib28","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1021\/acs.chemrev.7b00650","article-title":"Same substrate, many reactions: Oxygen activation in flavoenzymes","volume":"118","author":"Romero","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2021.101435_bib29","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1126\/science.aad4017","article-title":"Complementation of mitochondrial electron transport chain by manipulation of the NAD+\/NADH ratio","volume":"352","author":"Titov","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101435_bib30","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/nchembio.2454","article-title":"A\u00a0genetically encoded tool for manipulation of NADP(+)\/NADPH in living cells","volume":"13","author":"Cracan","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2021.101435_bib31","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.redox.2015.04.011","article-title":"Dimethyl fumarate modulates antioxidant and lipid metabolism in oligodendrocytes","volume":"5","author":"Huang","year":"2015","journal-title":"Redox Biol."},{"key":"10.1016\/j.jbc.2021.101435_bib32","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1038\/s41590-021-01048-3","article-title":"Mitochondrial complex II in intestinal epithelial cells regulates T cell-mediated immunopathology","volume":"22","author":"Fujiwara","year":"2021","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.jbc.2021.101435_bib33","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":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jbc.2021.101435_bib34","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0009-8981(81)90108-X","article-title":"Hypoxanthine production by ischemic heart demonstrated by high pressure liquid chromatography of blood purine nucleosides and oxypurines","volume":"115","author":"Harmsen","year":"1981","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.jbc.2021.101435_bib35","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1016\/j.celrep.2018.04.104","article-title":"Accumulation of succinate in cardiac ischemia primarily occurs via canonical Krebs cycle activity","volume":"23","author":"Zhang","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2021.101435_bib36","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1111\/j.1469-185X.1988.tb00632.x","article-title":"Operation of the purine nucleotide cycle in animal tissues","volume":"63","author":"van Waarde","year":"1988","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"10.1016\/j.jbc.2021.101435_bib37","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1111\/tra.12397","article-title":"Human fumarate hydratase is dual localized by an alternative transcription initiation mechanism","volume":"17","author":"Dik","year":"2016","journal-title":"Traffic"},{"key":"10.1016\/j.jbc.2021.101435_bib38","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/BF00972135","article-title":"Anion transport in rat brain mitochondria: Fumarate uptake via the dicarboxylate carrier","volume":"12","author":"Passarella","year":"1987","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.jbc.2021.101435_bib39","doi-asserted-by":"crossref","first-page":"7754","DOI":"10.1074\/jbc.RA118.001977","article-title":"The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS","volume":"293","author":"Maklashina","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib40","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0021-9258(18)70709-6","article-title":"Studies on succinic dehydrogenase. III. The fumaric reductase activity of succinic dehydrogenase","volume":"228","author":"Massey","year":"1957","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib41","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/S0021-9258(19)63680-X","article-title":"Studies on succinic dehydrogenase. VI. The reactivity of beef heart succinic dehydrogenase with electron carriers","volume":"229","author":"Massey","year":"1957","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib42","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1111\/j.1432-1033.1969.tb00640.x","article-title":"On the redox potentials of ubiquinone and cytochrome b in the respiratory chain","volume":"9","author":"Urban","year":"1969","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2021.101435_bib43","doi-asserted-by":"crossref","first-page":"7114","DOI":"10.1016\/S0021-9258(19)40916-2","article-title":"Mechanism of the reductive activation of succinate dehydrogenase","volume":"250","author":"Ackrell","year":"1975","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib44","doi-asserted-by":"crossref","first-page":"5577","DOI":"10.1016\/S0021-9258(19)69241-0","article-title":"Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase","volume":"256","author":"Ohnishi","year":"1981","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib45","doi-asserted-by":"crossref","first-page":"5989","DOI":"10.1128\/JB.180.22.5989-5996.1998","article-title":"Anaerobic expression of Escherichia coli succinate dehydrogenase: Functional replacement of fumarate reductase in the respiratory chain during anaerobic growth","volume":"180","author":"Maklashina","year":"1998","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2021.101435_bib46","doi-asserted-by":"crossref","first-page":"14887","DOI":"10.1021\/jacs.8b09022","article-title":"Spectroscopic and electronic structure study of ETHE1: Elucidating the factors influencing sulfur oxidation and oxygenation in mononuclear nonheme iron enzymes","volume":"140","author":"Goudarzi","year":"2018","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2021.101435_bib47","doi-asserted-by":"crossref","first-page":"12429","DOI":"10.1074\/jbc.RA118.004096","article-title":"Mechanism-based inhibition of human persulfide dioxygenase by gamma-glutamyl-homocysteinyl-glycine","volume":"293","author":"Kabil","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101435_bib48","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1101\/gad.191056.112","article-title":"Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors","volume":"26","author":"Xiao","year":"2012","journal-title":"Genes Dev."},{"key":"10.1016\/j.jbc.2021.101435_bib49","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/nchembio.495","article-title":"Identification of lysine succinylation as a new post-translational modification","volume":"7","author":"Zhang","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2021.101435_bib50","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.molcel.2013.06.001","article-title":"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways","volume":"50","author":"Park","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2021.101435_bib51","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1126\/science.1207861","article-title":"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase","volume":"334","author":"Du","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101435_bib52","doi-asserted-by":"crossref","first-page":"15560","DOI":"10.1073\/pnas.0705891104","article-title":"Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function","volume":"104","author":"Elrod","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101435_bib53","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.ccr.2012.02.014","article-title":"Metabolic reprogramming: A cancer hallmark even Warburg did not anticipate","volume":"21","author":"Ward","year":"2012","journal-title":"Cancer Cell"},{"key":"10.1016\/j.jbc.2021.101435_bib54","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40170-019-0202-2","article-title":"Tissue of origin dictates GOT1 dependence and confers synthetic lethality to radiotherapy","volume":"8","author":"Nelson","year":"2020","journal-title":"Cancer Metab."},{"key":"10.1016\/j.jbc.2021.101435_bib55","doi-asserted-by":"crossref","first-page":"6604","DOI":"10.1021\/acs.biochem.8b00914","article-title":"Biochemical characterization and structure-based mutational analysis provide insight into the binding and mechanism of action of novel aspartate aminotransferase inhibitors","volume":"57","author":"Holt","year":"2018","journal-title":"Biochemistry"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821012448?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821012448?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T20:52:19Z","timestamp":1777409539000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925821012448"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1]]},"references-count":55,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2022,1]]}},"alternative-id":["S0021925821012448"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101435","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2022,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A redox cycle with complex II prioritizes sulfide quinone oxidoreductase-dependent H2S oxidation","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101435","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 Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101435"}}