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In this work, the oxidation of trichloroethylene was studied with purified toluene 2-monooxygenase. All three purified toluene 2-monooxygenase protein components and NADH were required to reconstitute full trichloroethylene oxidation activity in vitro. The apparent Km and Vmax were 12 microM and 37 nmol per min per mg of hydroxylase component, respectively. Ten percent of the full activity was obtained when the small-molecular-weight enzyme component was omitted. The stable oxidation products, accounting for 84% of the trichloroethylene oxidized, were carbon monoxide, formic acid, glyoxylic acid, and covalently modified oxygenase proteins that constituted 12% of the reacted [14C]trichloroethylene. The stable oxidation products may all derive from the unstable intermediate trichloroethylene epoxide that was trapped by reaction with 4-(p-nitrobenzyl)pyridine. Chloral hydrate and dichloroacetic acid were not detected. This finding differs from that with soluble methane monooxygenase and cytochrome P-450 monooxygenase, which produce chloral hydrate. Trichloroethylene-dependent inactivation of toluene 2-monooxygenase activity was observed. All of the protein components were covalently modified during the oxidation of trichloroethylene. The addition of cysteine to reaction mixtures partially protected the enzyme system against inactivation, most notably protecting the NADH-oxidoreductase component. This suggested the participation of diffusible intermediates in the inactivation of the oxidoreductase.<\/jats:p>","DOI":"10.1128\/jb.179.1.90-96.1997","type":"journal-article","created":{"date-parts":[[2016,11,10]],"date-time":"2016-11-10T14:52:20Z","timestamp":1478789540000},"page":"90-96","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":66,"title":["Trichloroethylene oxidation by purified toluene 2-monooxygenase: products, kinetics, and turnover-dependent inactivation"],"prefix":"10.1128","volume":"179","author":[{"given":"L M","family":"Newman","sequence":"first","affiliation":[{"name":"Department of Biochemistry, the Biological Process Technology Institute, University of Minnesota, St. Paul 55108, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L P","family":"Wackett","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, the Biological Process Technology Institute, University of Minnesota, St. Paul 55108, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1016\/0006-2952(80)90022-2","article-title":"The mechanism of chloroform and carbon monooxide formation from carbon tetrachloride by microsomal cytochrome P-450","volume":"29","author":"Ahr H. 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