{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T03:14:15Z","timestamp":1790997255951,"version":"4.1.0"},"reference-count":34,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"6208","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2014,10,24]]},"abstract":"<jats:title>How bacteria break down organohalides<\/jats:title>\n                  <jats:p>\n                    Anaerobic bacteria can break down a range of organohalide pollutants. To do so, they use unusual reductive dehalogenase enzymes that remove the halogen ion from the molecule, making the pollutants less toxic. Bommer\n                    <jats:italic>et al.<\/jats:italic>\n                    describe x-ray crystal structures of one such enzyme from\n                    <jats:italic>Sulfurospirillum multivorans<\/jats:italic>\n                    (see the Perspective by Edwards). Vitamin B\n                    <jats:sub>12<\/jats:sub>\n                    , present near the substrate binding site, catalyzes the reduction of trichloroethylene in concert with two iron-sulfur clusters. The structures provide mechanistic clues for how to engineer enzymes to recognize other pollutants.\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=\"6208\" page=\"455\" related-article-type=\"in-this-issue\" vol=\"346\" xlink:href=\"10.1126\/science.1258118\">455<\/jats:related-article>\n                    ; see also p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6208\" page=\"424\" related-article-type=\"in-this-issue\" vol=\"346\" xlink:href=\"10.1126\/science.1261194\">424<\/jats:related-article>\n                  <\/jats:p>","DOI":"10.1126\/science.1258118","type":"journal-article","created":{"date-parts":[[2014,10,2]],"date-time":"2014-10-02T22:23:21Z","timestamp":1412288601000},"page":"455-458","source":"Crossref","is-referenced-by-count":266,"title":["Structural basis for organohalide respiration"],"prefix":"10.1126","volume":"346","author":[{"given":"Martin","family":"Bommer","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Biologie, Strukturbiologie\/Biochemie, Humboldt-Universit\u00e4t zu Berlin, Unter den Linden 6, 10099 Berlin, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cindy","family":"Kunze","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Mikrobiologie, Friedrich-Schiller-Universit\u00e4t Jena, Lehrstuhl f\u00fcr Angewandte und \u00d6kologische Mikrobiologie, Philosophenweg 12, 07743 Jena, 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