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Title: Anaerobic aryl reductive dehalogenation of halobenzoates by cell extracts of Desulfomonile tiedjei

Journal Article · · Applied and Environmental Microbiology; (United States)
OSTI ID:5462690

The authors studied the transformation of halogenated benzoates by cell extracts of a dehalogenating anaerobe, Desulfomonile tiedjei. The authors found that cell extracts possessed aryl reductive dehalogenation activity. The activity was heat labile and dependent on the addition of reduced methyl viologen, but not on that of reduced NAD, NADP, flavin mononucleotide, flavin adenine dinucleotide, desulfoviridin, cytochrome c{sub 3}, or benzyl viologen. Dehalogenation activity in extracts was stimulated by formate, CO, or H{sub 2}, but not by pyruvate plus coenzyme A or by dithionite. The pH and temperature optima for aryl dehalogenation were 8.2 and 35{degree}C, respectively. The rate of dehalogenation was proportional to the amount of protein in the assay mixture. The substrate specificity of aryl dehalogenation activity for various aromatic compounds in D. tiedjei cell extracts was identical to that of whole cells, except differences were observed in the relative rates of halobenzoate transformation. Dehalogenation was 10-fold greater in D. tiedjei extracts prepared from cells cultured in the presence of 3-chlorobenzoate, suggesting that the activity was inducible. Aryl reductive dehalogenation in extracts was inhibited by sulfite, sulfide, and thiosulfate, but not sulfate. Experiments with combinations of substrates suggested that cell extracts dehalogenated 3-iodobenzoate more readily than either 3,5-dichlorobenzoate or 3-chlorobenzoate. Dehalogenation activity was found to be membrane associated. This is the first report characterizing aryl dehalogenation activity in cell extracts of an obligate anaerobe.

OSTI ID:
5462690
Journal Information:
Applied and Environmental Microbiology; (United States), Vol. 56:10; ISSN 0099-2240
Country of Publication:
United States
Language:
English