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dc.contributor.authorBlasco, Rafael
dc.contributor.authorRamos, Juan-Luis
dc.contributor.authorWittich, Rolf-Michael
dc.date.accessioned2008-06-23T14:07:51Z
dc.date.available2008-06-23T14:07:51Z
dc.date.issued2008-06
dc.identifier.citationPseudomonas aeruginosa strain RW41 mineralizes 4-chlorobenzenesulfonate, the major polar by-product from DDT manufacturing. 2008, 10 (6):1591-600 Environ. Microbiol.en
dc.identifier.issn1462-2920
dc.identifier.pmid18331335
dc.identifier.doi10.1111/j.1462-2920.2008.01575.x
dc.identifier.urihttp://hdl.handle.net/10033/30324
dc.description.abstractPseudomonas aeruginosa RW41 is the first bacterial strain, which could be isolated by virtue of its capability to mineralize 4-chlorobenzenesulfonic acid (4CBSA), the major polar by-product of the chemical synthesis of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT). This capability makes the isolate a promising candidate for the development of bioremediation technologies. The bacterial mineralization of 4CBSA proceeds under oxygenolytic desulfonation and transient accumulation of sulfite which then is oxidized to sulfate. High enzyme activities for the turnover of 4-chlorocatechol were measured. The further catabolism proceeded through 3-chloromuconate and, probably, the instable 4-chloromuconolactone, which is directly hydrolyzed to maleylacetate. Detectable levels of maleylacetate reductase were only present when cells were grown with 4CBSA. When the ordinary catechol pathway was induced during growth on benzenesulfonate, catechol was ortho-cleaved to cis,cis-muconate and a partially purified muconate cycloisomerase transformed it to muconolactone in vitro. The same enzyme transformed 3-chloro-cis,cis-muconate into cis-dienelactone (76%) and the antibiotically active protoanemonin (24%). These observations are indicative for a not yet highly evolved catabolism for halogenated substrates by bacterial isolates from environmental samples which, on the other hand, are able to productively recycle sulfur and chloride ions from synthetic haloorganosulfonates.
dc.language.isoenen
dc.subject.meshBenzenesulfonatesen
dc.subject.meshCatecholsen
dc.subject.meshChromatography, Ion Exchangeen
dc.subject.meshDDTen
dc.subject.meshFuransen
dc.subject.meshHydrocarbons, Halogenateden
dc.subject.meshIntramolecular Lyasesen
dc.subject.meshLactonesen
dc.subject.meshMaleatesen
dc.subject.meshMetabolic Networks and Pathwaysen
dc.subject.meshOxidation-Reductionen
dc.subject.meshPseudomonas aeruginosaen
dc.subject.meshSorbic Aciden
dc.subject.meshSulfatesen
dc.subject.meshSulfitesen
dc.titlePseudomonas aeruginosa strain RW41 mineralizes 4-chlorobenzenesulfonate, the major polar by-product from DDT manufacturing.en
dc.typeArticleen
dc.contributor.departmentDepartamento de Bioquímica, Biología Molecular y Genética, Facultad de Veterinaria, Universidad de Extremadura, E-10071 Cáceres, Spain.en
dc.identifier.journalEnvironmental microbiologyen
refterms.dateFOA2009-06-05T00:00:00Z
html.description.abstractPseudomonas aeruginosa RW41 is the first bacterial strain, which could be isolated by virtue of its capability to mineralize 4-chlorobenzenesulfonic acid (4CBSA), the major polar by-product of the chemical synthesis of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT). This capability makes the isolate a promising candidate for the development of bioremediation technologies. The bacterial mineralization of 4CBSA proceeds under oxygenolytic desulfonation and transient accumulation of sulfite which then is oxidized to sulfate. High enzyme activities for the turnover of 4-chlorocatechol were measured. The further catabolism proceeded through 3-chloromuconate and, probably, the instable 4-chloromuconolactone, which is directly hydrolyzed to maleylacetate. Detectable levels of maleylacetate reductase were only present when cells were grown with 4CBSA. When the ordinary catechol pathway was induced during growth on benzenesulfonate, catechol was ortho-cleaved to cis,cis-muconate and a partially purified muconate cycloisomerase transformed it to muconolactone in vitro. The same enzyme transformed 3-chloro-cis,cis-muconate into cis-dienelactone (76%) and the antibiotically active protoanemonin (24%). These observations are indicative for a not yet highly evolved catabolism for halogenated substrates by bacterial isolates from environmental samples which, on the other hand, are able to productively recycle sulfur and chloride ions from synthetic haloorganosulfonates.


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