{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T17:26:16Z","timestamp":1773249976246,"version":"3.50.1"},"reference-count":40,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"6267","license":[{"start":{"date-parts":[[2016,12,18]],"date-time":"2016-12-18T00:00:00Z","timestamp":1482019200000},"content-version":"vor","delay-in-days":366,"URL":"http:\/\/www.sciencemag.org\/about\/science-licenses-journal-article-reuse"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2015,12,18]]},"abstract":"<jats:title>Sulfate reduction via a trisulfide<\/jats:title>\n          <jats:p>\n            Microorganisms can respire sulfur compounds in the absence of oxygen, eventually leading to the production of hydrogen sulfide. This ancient metabolism is common in modern anoxic environments, but the enzymatic pathways aren't yet fully resolved. Through in vivo and in vitro experiments, Santos\n            <jats:italic>et al.<\/jats:italic>\n            clarify the enzymology of the sulfate reduction pathway in both bacteria and archaea (see the Perspective by Fritz and Kroneck). Reduction of the sulfite intermediate results in the linkage of two cysteine residues to a third sulfur atom from sulfite, forming a trisulfide product. Because the reduction of sulfite conveys a strong isotopic signature on sulfur in the environment, isotope fractionation models should account for this additional step.\n          <\/jats:p>\n          <jats:p>\n            <jats:italic>Science<\/jats:italic>\n            , this issue p.\n            <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6267\" page=\"1541\" related-article-type=\"in-this-issue\" vol=\"350\" xlink:href=\"10.1126\/science.aad3558\">1541<\/jats:related-article>\n            ; see also p.\n            <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6267\" page=\"1476\" related-article-type=\"in-this-issue\" vol=\"350\" xlink:href=\"10.1126\/science.aad8139\">1476<\/jats:related-article>\n          <\/jats:p>","DOI":"10.1126\/science.aad3558","type":"journal-article","created":{"date-parts":[[2015,12,17]],"date-time":"2015-12-17T21:11:05Z","timestamp":1450386665000},"page":"1541-1545","source":"Crossref","is-referenced-by-count":238,"title":["A protein trisulfide couples dissimilatory sulfate reduction to energy conservation"],"prefix":"10.1126","volume":"350","author":[{"given":"Andr\u00e9 A.","family":"Santos","sequence":"first","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal."}]},{"given":"Sofia S.","family":"Venceslau","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal."}]},{"given":"Fabian","family":"Grein","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal."}]},{"given":"William D.","family":"Leavitt","sequence":"additional","affiliation":[{"name":"Department of Earth and Planetary Science, Harvard University, Cambridge, MA, USA."}]},{"given":"Christiane","family":"Dahl","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Mikrobiologie &amp; Biotechnologie, Rheinische Friedrich-Wilhelms-Universit\u00e4t Bonn, Germany."}]},{"given":"David T.","family":"Johnston","sequence":"additional","affiliation":[{"name":"Department of Earth and Planetary Science, Harvard University, Cambridge, MA, USA."}]},{"given":"In\u00eas A. 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