{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,12]],"date-time":"2026-04-12T19:22:49Z","timestamp":1776021769124,"version":"3.50.1"},"reference-count":45,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,10,27]],"date-time":"2006-10-27T00:00:00Z","timestamp":1161907200000},"content-version":"vor","delay-in-days":6569,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[1988,11]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The nucleotide sequence of a 6.5 kilobasepair chromosomal DNA fragment encoding the anaerobic dimethylsulphoxide (DMSO) reductase operon of <jats:italic>Escherichia coli<\/jats:italic> has been determined. The DMSO reductase structural operon was shown to consist of three open reading frames, namely <jats:italic>dmsABC<\/jats:italic>, encoding polypeptides with predicted molecular weights of 87350, 23070, and 30789 Daltons, respectively. The DMS A polypeptide displayed a high degree of amino acid sequence homology with the single\u2010subunit enzyme, biotin sulphoxide reductase (<jats:italic>bisC<\/jats:italic>) and with formate dehydrogenase (<jats:italic>fdhF<\/jats:italic>), suggesting that the active site and molybdopterin cofactor binding site that is common to these enzymes is located in the DMS A subunit. A comparison of the predicted <jats:italic>N<\/jats:italic>\u2010terminal amino acids of the <jats:italic>dmsA<\/jats:italic> gene product to those of the 82600 subunit of purified DMSO reductase indicated that post\u2010translational processing of a 16 amino acid peptide at the amino terminus of DMS A had occurred. The DMS B polypeptide contains 16 cysteine residues organized in four clusters, two of which are typical of 4Fe\u20134S binding domains. The DMS C polypeptide is composed of eight segments of hydrophobic amino acids of appropriate length to cross the cytoplasmic membrane, suggesting that this subunit functions to anchor the enzyme to the membrane.<\/jats:p>","DOI":"10.1111\/j.1365-2958.1988.tb00090.x","type":"journal-article","created":{"date-parts":[[2006,10,27]],"date-time":"2006-10-27T20:48:12Z","timestamp":1161982092000},"page":"785-795","source":"Crossref","is-referenced-by-count":133,"title":["Nucleotide sequence of the <i>dmsABC<\/i> operon encoding the anaerobic dimethylsulphoxide reductase of <i>Escherichia coli<\/i>"],"prefix":"10.1111","volume":"2","author":[{"given":"P. T.","family":"Bilous","sequence":"first","affiliation":[]},{"given":"S. T.","family":"Cole","sequence":"additional","affiliation":[]},{"given":"W. 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