1987Applied and Environmental MicrobiologyOpen access

Degradation of 1,4-dichlorobenzene by a Pseudomonas sp

Jim C. Spain, Shirley F. Nishino

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Abstract

A Pseudomonas species able to degrade p-dichlorobenzene as the sole source of carbon and energy was isolated by selective enrichment from activated sludge. The organism also grew well on chlorobenzene and benzene. Washed cells released chloride in stoichiometric amounts from o-, m-, and p-dichlorobenzene, 2,5-dichlorophenol, 4-chlorophenol, 3-chlorocatechol, 4-chlorocatechol, and 3,6-dichlorocatechol. Initial steps in the pathway for p-dichlorobenzene degradation were determined by isolation of metabolites, simultaneous adaptation studies, and assay of enzymes in cell extracts. Results indicate that p-dichlorobenzene was initially converted by a dioxygenase to 3,6-dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene, which was converted to 3,6-dichlorocatechol by an NAD+-dependent dehydrogenase. Ring cleavage of 3,6-dichlorocatechol was by a 1,2-oxygenase to form 2,5-dichloro-cis, cis-muconate. Enzymes for degradation of haloaromatic compounds were induced in cells grown on chlorobenzene or p-dichlorobenzene, but not in cells grown on benzene, succinate, or yeast extract. Enzymes of the ortho pathway induced in cells grown on benzene did not attack chlorobenzenes or chlorocatechols.

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What this paper is about

A Pseudomonas species able to degrade p-dichlorobenzene as the sole source of carbon and energy was isolated by selective enrichment from activated sludge. The organism also grew well on chlorobenzene and benzene. Washed cells released chloride in stoichiometric amounts from o-, m-, and p-dichlorobenzene, 2,5-dichlorophenol, 4-chlorophenol, 3-chlorocatechol, 4-chlorocatechol, and 3,6-dichlorocatechol. Initial steps in the pathway for p-dichlorobenzene degradation were determined by isolation of metabolites, simultaneous adaptation studies, and assay of enzymes in cell extracts. Results indicate that p-dichlorobenzene was initially converted by a dioxygenase to 3,6-dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene, which was converted to 3,6-dichlorocatechol by an NAD+-dependent dehydrogenase. Ring cleavage of 3,6-dichlorocatechol was by a 1,2-oxygenase to form 2,5-dichloro-cis, cis-muconate. Enzymes for degradation of haloaromatic compounds were induced in cells grown on chlorobenzene or p-dichlorobenzene, but not in cells grown on benzene, succinate, or yeast extract. Enzymes of the ortho pathway induced in cells grown on benzene did not attack chlorobenzenes or chlorocatechols.

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Available abstract

A Pseudomonas species able to degrade p-dichlorobenzene as the sole source of carbon and energy was isolated by selective enrichment from activated sludge. The organism also grew well on chlorobenzene and benzene. Washed cells released chloride in stoichiometric amounts from o-, m-, and p-dichlorobenzene, 2,5-dichlorophenol, 4-chlorophenol, 3-chlorocatechol, 4-chlorocatechol, and 3,6-dichlorocatechol. Initial steps in the pathway for p-dichlorobenzene degradation were determined by isolation of metabolites, simultaneous adaptation studies, and assay of enzymes in cell extracts. Results indicate that p-dichlorobenzene was initially converted by a dioxygenase to 3,6-dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene, which was converted to 3,6-dichlorocatechol by an NAD+-dependent dehydrogenase. Ring cleavage of 3,6-dichlorocatechol was by a 1,2-oxygenase to form 2,5-dichloro-cis, cis-muconate. Enzymes for degradation of haloaromatic compounds were induced in cells grown on chlorobenzene or p-dichlorobenzene, but not in cells grown on benzene, succinate, or yeast extract. Enzymes of the ortho pathway induced in cells grown on benzene did not attack chlorobenzenes or chlorocatechols.

Key concepts: Chlorobenzene, Benzene, Dichlorobenzene, Chemistry, Enzyme, Dehydrogenase, Biodegradation, Pentachlorophenol

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