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Cytochrome P450_CAM from Pseudomonas putida G786 oxidized chlorinated ethanes and 1,2-dichloropropane. The rate of NADH oxidation decreased with decreasing chlorine substitution. The single detectable oxidation products of 1,1,1-trichloroethane and 1,2-dichloropropane were 1,1,1-trichloroethanol and chloroacetone, respectively. Organic product formation was largely uncoupled from NADH oxidation.Copyright 1994, 1999 Academic Press, Inc.

Pseudomonas aeruginosa strain 142 oxidizes 2-halobenzoates via a multicomponent oxygenase (V.Romanov and R.P. Hausinger, J. Bacteriol., 1994, 176(11), 3368-3374). The intermediacy of a highly unstable cis-diol in the reaction has been proposed. Direct evidence for this is currently lacking and the stereochemical course of the reaction cannot be inferred from previous studies. In this study, 2-trifluoromethylbenzoate was stoichiometrically oxidized by P. aeruginosa 142 to a chiral product identified as (−)2-trifluoromethyl-cis-1,2-dihydroxy-3, acid. These data rigorously establish a dioxygenative mechanism for 2-halobenzoate metabolism.Copyright 1995, 1999 Academic Press, Inc.

Distinct dichloromethane dehalogenases from Methylobacteriumsp. strain DM4 and MethylophilusDM11 were inhibited by low concentrations of haloacetonitriles. Chloroacetonitrile (ClCH2CN) showed maximal inhibition at a stoichiometry of 1 mol inhibitor: 1 mol holoenzyme for both enzymes. This stoichiometry is suggestive of one active site per holoenzyme or extreme negative cooperativity amongst the subunits. Radiolahcllcd ClCH2CN dissociated completely or partially from the two dehalogenases, respectively, during chromatography. This suggested ClCH2CN was bound non-covalently.