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J. Bacteriol., 06 1997, 3858-3865, Vol 179, No. 12
Copyright © 1997, American Society for Microbiology

Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification

CC Lange and LP Wackett
Department of Biochemistry, Biological Process Technology Institute, and Center for Biodegradation Research and Informatics, University of Minnesota, St. Paul 55108, USA.

Toluene dioxygenase from Pseudomonas putida F1 has been studied extensively with aromatic substrates. The present work examined the toluene dioxygenase-catalyzed oxidation of various halogenated ethenes, propenes, butenes and nonhalogenated cis-2-pentene, an isomeric mix of 2-hexenes, cis-2-heptene, and cis-2-octene as substrates for toluene dioxygenase. Enzyme specific activities were determined for the more water-soluble C2 to C5 compounds and ranged from <4 to 52 nmol per min per mg of protein. Trichloroethene was oxidized at a rate of 33 nmol per min per mg of protein. Products from enzyme reactions were identified by gas chromatography-mass spectrometry. Proton and carbon nuclear magnetic resonance spectroscopy of compounds from whole-cell incubation confirmed the identity of products. Substrates lacking a halogen substituent on sp2 carbon atoms were dioxygenated, while those with halogen and one or more unsubstituted allylic methyl groups were monooxygenated to yield allylic alcohols. 2,3-Dichloro-1-propene, containing both a halogenated double bond and a halogenated allylic methyl group, underwent monooxygenation with allylic rearrangement to yield an isomeric mixture of cis- and trans-2,3-dichloro-2-propene-1-ol.


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