Oxidation of trichloroethylene, 1,1-dichloroethylene, and chloroform by toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1.
Toluene/o-xylene monooxygenase (ToMO) from Pseudomonas stutzeri OX1, which oxidizes toluene and o-xylene, was examined for its ability to degrade the environmental pollutants trichloroethylene (TCE), 1, 1-dichloroethylene (1,1-DCE), cis-1,2-DCE, trans-1,2-DCE, chloroform, dichloromethane, phenol, 2,4-dichlorophenol, 2,4,5-trichlorophenol, 2,4,6-trichlorophenol, 2,3,5,6-tetrachlorophenol, and 2,3,4,5, 6-pentachlorophenol. Escherichia coli JM109 that expressed ToMO from genes on plasmid pBZ1260 under control of the lac promoter degraded TCE (3.3 microM), 1,1-DCE (1.25 microM), and chloroform (6.3 microM) at initial rates of 3.1, 3.6, and 1.6 nmol/(min x mg of protein), respectively. Stoichiometric amounts of chloride release were seen, indicating mineralization (2.6, 1.5, and 2.3 Cl- atoms per molecule of TCE, 1,1-DCE, and chloroform, respectively). Thus, the substrate range of ToMO is extended to include aliphatic chlorinated compounds.
Department of Chemical and Biochemical Engineering, University of California, Irvine, California 92697-2575, USA.
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Chauhan
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Barbieri
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Wood
D001673:Biodegradation, Environmental; D002712:Chlorides / Q000378:metabolism; D002725:Chloroform / Q000378:metabolism*; D004000:Dichloroethylenes / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D014241:Trichloroethylene / Q000378:metabolism*
D002712:Chlorides; D004000:Dichloroethylenes; D011994:Recombinant Proteins; C029297:vinylidene chloride; D014241:Trichloroethylene; D002725:Chloroform; D010105:Oxygenases; C114360:toluene 2-xylene monooxygenase