Oxidation of chlorinated olefins by Escherichia coli transformed with dimethyl sulfide monooxygenase genes or cumene dioxygenase genes

In the present work, it was shown that the dimethyl sulfide (DMS) monooxyge nase and the cumene dioxygenase catalyzed oxidation of various chlorinated ethenes, propenes, and butenes. The specific activities of these oxygenases were determined for C-2 to C-4 chlorinated olefins, and the oxidation rate s ranged from 0.19 to 4.18 nmol . min(-1) . mg(-1) of dry cells by the DMS monooxygenase and from 0.19 to 1.29 nmol . min(-1) . mg(-1) of dry cells by the cumene dioxygenase. The oxidation products were identified by gas chro matography-mass spectrometry. Most chlorinated olefins were monooxygenated by the DMS monooxygenase to yield chlorinated epoxides. In the case of the cumene dioxygenase, the substrates lacking any chlorine atom on double-bond carbon atoms were dioxygenated, and those with chlorine atoms attaching to double-bond carbon atoms were monooxygenated to yield allyl alcohols.