Aerobic cometabolism of cis-1,2-dichloroethylene (c-DCE) by a butane-grown mixed culture was evaluated in batch kinetic tests. The transformation of c-DCE resulted in the coincident generation of c-DCE epoxide. Chloride release studies showed ∼75% oxidative dechlorination of c-DCE. Mass spectrometry confirmed the presence of a compound with mass-to-charge-fragment ratios of 112, 83, 48, and 35. These values are in agreement with the spectra of chemically synthesized c-DCE epoxide. The transformation of c-DCE required O2, was inhibited by butane and was inactivated by acetylene (a known monooxygenase inactivator), indicating that a butane monooxygenase enzyme was likely involved in the transformation of c-DCE. This study showed c-DCE epoxide was biologically transformed, likely by a butane monooxygenase enzyme. c-DCE epoxide transformation was inhibited by both acetylene and c-DCE indicating a monooxygenase enzyme was involved. The epoxide transformation was also stopped when mercuric chloride (HgCl2) was added as a biological inhibitor, further support a biological transformation. To our knowledge this is the first report of the biological transform c-DCE epoxide by a butane-grown culture.

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