{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T11:46:30Z","timestamp":1790077590615,"version":"4.0.1"},"reference-count":33,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2017,6,20]],"date-time":"2017-06-20T00:00:00Z","timestamp":1497916800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microbial Biotechnology"],"published-print":{"date-parts":[[2017,11]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    We report herein the purification of a chloroform (\n                    <jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content>\n                    )\u2010reducing enzyme, TmrA, from the membrane fraction of a strict anaerobe\n                    <jats:italic>Dehalobacter<\/jats:italic>\n                    sp. strain\n                    <jats:styled-content style=\"fixed-case\">UNSWDHB<\/jats:styled-content>\n                    to apparent homogeneity with an approximate 23\u2010fold increase in relative purity compared to crude lysate. The membrane fraction obtained by ultracentrifugation was solubilized in Triton X\u2010100 in the presence of glycerol, followed by purification by anion exchange chromatography. The molecular mass of the purified TmrA was determined to be 44.5\n                    <jats:styled-content style=\"fixed-case\">kD<\/jats:styled-content>\n                    a by\n                    <jats:styled-content style=\"fixed-case\">SDS<\/jats:styled-content>\n                    \u2010\n                    <jats:styled-content style=\"fixed-case\">PAGE<\/jats:styled-content>\n                    and MALDI\u2010TOF\/TOF. The purified dehalogenase reductively dechlorinated\n                    <jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content>\n                    to dichloromethane\n                    <jats:italic>in\u00a0vitro<\/jats:italic>\n                    with reduced methyl viologen as the electron donor at a specific activity of (1.27\u00a0\u00b1\u00a00.04)\u00a0\u00d7\u00a010\n                    <jats:sup>3<\/jats:sup>\n                    units\u00a0mg protein\n                    <jats:sup>\u22121<\/jats:sup>\n                    . The optimum temperature and\n                    <jats:styled-content style=\"fixed-case\">pH<\/jats:styled-content>\n                    for the activity were 45\u00b0C and 7.2, respectively. The\n                    <jats:styled-content style=\"fixed-case\">UV<\/jats:styled-content>\n                    \u2010visible spectrometric analysis indicated the presence of a corrinoid and two [4Fe\u20104S] clusters, predicted from the amino acid sequence. This is the first report of the production, purification and biochemical characterization of a CF reductive dehalogenase.\n                  <\/jats:p>","DOI":"10.1111\/1751-7915.12745","type":"journal-article","created":{"date-parts":[[2017,6,20]],"date-time":"2017-06-20T04:38:39Z","timestamp":1497933519000},"page":"1640-1648","source":"Crossref","is-referenced-by-count":34,"title":["A bacterial chloroform reductive dehalogenase: purification and biochemical characterization"],"prefix":"10.1111","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8893-1170","authenticated-orcid":false,"given":"Bat\u2010Erdene","family":"Jugder","sequence":"first","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susanne","family":"Bohl","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"},{"name":"Department of Biotechnology Mannheim University of Applied Sciences 68163 Mannheim Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helene","family":"Lebhar","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert D.","family":"Healey","sequence":"additional","affiliation":[{"name":"School of Chemistry University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mike","family":"Manefield","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1656-7215","authenticated-orcid":false,"given":"Christopher P.","family":"Marquis","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew","family":"Lee","sequence":"additional","affiliation":[{"name":"School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW 2052 Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2017,6,20]]},"reference":[{"key":"e_1_2_7_2_1","unstructured":"ASTDR(2015).Toxological profile for chloroform. 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