{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T20:11:43Z","timestamp":1790712703708,"version":"4.1.0"},"reference-count":10,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,1,27]],"date-time":"2022-01-27T00:00:00Z","timestamp":1643241600000},"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":["GM61606"],"award-info":[{"award-number":["GM61606"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000738","name":"U.S. Department of Veterans Affairs","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000738","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":[[2022,3]]},"DOI":"10.1016\/j.jbc.2022.101661","type":"journal-article","created":{"date-parts":[[2022,1,29]],"date-time":"2022-01-29T19:06:26Z","timestamp":1643483186000},"page":"101661","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Complexities of complex II: Sulfide metabolism in\u00a0vivo"],"prefix":"10.1016","volume":"298","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0571-1747","authenticated-orcid":false,"given":"Gary","family":"Cecchini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.101661_bib1","doi-asserted-by":"crossref","first-page":"R1177","DOI":"10.1016\/j.cub.2017.09.015","article-title":"The origin and diversification of mitochondria","volume":"27","author":"Roger","year":"2017","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2022.101661_bib2","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1002\/bies.201400060","article-title":"Of early animals, anaerobic mitochondria, and a modern sponge","volume":"36","author":"Mentel","year":"2014","journal-title":"Bioessays"},{"key":"10.1016\/j.jbc.2022.101661_bib3","doi-asserted-by":"crossref","first-page":"101435","DOI":"10.1016\/j.jbc.2021.101435","article-title":"A\u00a0redox cycle with complex II prioritizes sulfide quinone oxidoreductase dependent H2S oxidation","volume":"298","author":"Kumar","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.101661_bib4","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.2022.101661_bib5","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.2022.101661_bib6","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.2022.101661_bib7","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.2022.101661_bib8","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.2022.101661_bib9","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1126\/science.abi7495","article-title":"Fumarate is a terminal electron acceptor in the mammalian electron transport chain","volume":"374","author":"Spinelli","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.101661_bib10","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1038\/s41467-018-04603-z","article-title":"Alternative assembly of respiratory complex II connects energy stress to metabolic checkpoints","volume":"9","author":"Bezawork-Geleta","year":"2018","journal-title":"Nat. Commun."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822001016?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822001016?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:10:12Z","timestamp":1758240612000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925822001016"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3]]},"references-count":10,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2022,3]]}},"alternative-id":["S0021925822001016"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.101661","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2022,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Complexities of complex II: Sulfide metabolism in\u00a0vivo","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.101661","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101435","name":"associatedlink","label":"CrossRef DOI link to the associated document"},{"value":"simple-article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101661"}}