Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol

Dorn, Emmi; Knackmuss, Hans‐Joachim

doi:10.1042/bj1740085

Cited by 331 publications

(228 citation statements)

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“…Only a few proteobacterial catechol 1,2-dioxygenases have been described in detail for their catabolic properties. In all cases reported to date, catechol is the preferred substrate, as indicated by specificity constants of 30-to 100-fold that of 4-chlorocatechol (10, 52) and 6-to 40-fold that of 4-methylcatechol (10,52,62). C12O salD of MT1 is particular in this respect; its specificity constants for catechol and 4-chlorocatechol are similar, and of the substrates tested, 4-methylcatechol is the preferred substrate.…”

Section: Discussionmentioning

confidence: 91%

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

et al. 2007

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Pseudomonas sp. strain MT1 has recently been reported to degrade 4-and 5-chlorosalicylate by a pathway assumed to consist of a patchwork of reactions comprising enzymes of the 3-oxoadipate pathway. Genes encoding the initial steps in the degradation of salicylate and substituted derivatives were now localized and sequenced. One of the gene clusters characterized (sal) showed a novel gene arrangement, with salA, encoding a salicylate 1-hydroxylase, being clustered with salCD genes, encoding muconate cycloisomerase and catechol 1,2-dioxygenase, respectively, and was expressed during growth on salicylate and chlorosalicylate. A second gene cluster (cat), exhibiting the typical catRBCA arrangement of genes of the catechol branch of the 3-oxoadipate pathway in Pseudomonas strains, was expressed during growth on salicylate. Despite their high sequence similarities with isoenzymes encoded by the cat gene cluster, the catechol 1,2-dioxygenase and muconate cycloisomerase encoded by the sal cluster showed unusual kinetic properties. Enzymes were adapted for turnover of 4-chlorocatechol and 3-chloromuconate; however, 4-methylcatechol and 3-methylmuconate were identified as the preferred substrates. Investigation of the substrate spectrum identified 4-and 5-methylsalicylate as growth substrates, which were effectively converted by enzymes of the sal cluster into 4-methylmuconolactone, followed by isomerization to 3-methylmuconolactone. The function of the sal gene cluster is therefore to channel both chlorosubstituted and methylsubstituted salicylates into a catechol ortho cleavage pathway, followed by dismantling of the formed substituted muconolactones through specific pathways.

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Section: Discussionmentioning

confidence: 91%

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

et al. 2007

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“…This conclusion suggests an analogy between degradation of aromatic compounds via catechol or chlorocatechol and degradation via hydroxyquinol or chlorohydroxyquinol. The channeling of catechol and chlorocatechol into the 3-oxoadipate pathway by the respective enzymes has been described in detail elsewhere (9,10,17,23,(28)(29)(30)(31)(32)37). The majority of these studies raise the question of the evolution of the modified ortho-cleavage pathway for chlorocatechol degradation and also speculate about an analogy with the ortho-cleavage pathway for the degradation of nonchlorinated catechol.…”

Section: Resultsmentioning

confidence: 99%

“…Two pathways for the aerobic degradation of chlorophenols have been described so far: one via chlorocatechols and the other via chlorohydroquinones (2,9,10,15). A predominant catabolic route for the compounds carrying one or two chlorine substituents was shown to be the modified ortho-cleavage pathway (14,18,24).…”

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confidence: 99%

Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1

et al. 1995

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The enzyme which cleaves the benzene ring of 6-chlorohydroxyquinol was purified to apparent homogeneity from an extract of 2,4,6-trichlorophenol-grown cells of Streptomyces rochei 303. Like the analogous enzyme from Azotobacter sp. strain GP1, it exhibited a highly restricted substrate specificity and was able to cleave only 6-chlorohydroxyquinol and hydroxyquinol and not catechol, chlorinated catechols, or pyrogallol. No extradiolcleaving activity was observed. In contrast to 6-chlorohydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1, the S. rochei enzyme had a distinct preference for 6-chlorohydroxyquinol over hydroxyquinol (k cat /K m ‫؍‬ 1.2 and 0.57 s ؊1 ⅐ M ؊1 , respectively). The enzyme from S. rochei appears to be a dimer of two identical 31-kDa subunits. It is a colored protein and was found to contain 1 mol of iron per mol of enzyme. The NH 2 -terminal amino acid sequences of 6-chlorohydroxyquinol 1,2-dioxygenase from S. rochei 303 and from Azotobacter sp. strain GP1 showed a high degree of similarity.Two pathways for the aerobic degradation of chlorophenols have been described so far: one via chlorocatechols and the other via chlorohydroquinones (2, 9, 10, 15). A predominant catabolic route for the compounds carrying one or two chlorine substituents was shown to be the modified ortho-cleavage pathway (14,18,24). In this pathway, chlorocatechols formed by introduction of a second hydroxy group are subjected to intradiol cleavage. In the case of chlorophenol degradation through the chlorohydroquinone pathway, the introduction of a third hydroxy group leads to the formation of hydroxyquinol or chlorohydroxyquinol (3, 13). Both unsubstituted and chlorinated 1,2,4-trihydroxybenzene were shown to be subject to ortho cleavage in Streptomyces rochei 303 (13). Extracts from cells grown in the presence of 2-chloro-or 2,4-dichlorophenol were found to prefer hydroxyquinol over 6-chlorohydroxyquinol as a ring fission substrate, whereas extracts from cells grown on 2,6-dichloro-or 2,4,6-trichlorophenol showed a preference for the chlorinated substrate (13). These results led us to suggest that two different dioxygenases play a role in the cleavage of the trihydroxylated aromatic ring: 6-chlorohydroxyquinol 1,2-dioxygenase in the ring fission of 6-chlorohydroxyquinol, the proposed intermediate of 2,4,6-trichloro-and 2,6-dichlorophenol degradation, and a second dioxygenase in the cleavage of hydroxyquinol, the proposed intermediate of 2,4-dichloro-and 2-chlorophenol degradation (Fig. 1) (13).In this paper, we describe the purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase. Three other hydroxyquinol 1,2-dioxygenases have been purified and characterized so far (21,25,34). One of them takes part in the cleavage of hydroxyquinol, found as an intermediate of 4-hydroxybenzoate degradation in Trichosporon cutaneum (34).The second dioxygenase, from the basidiomycete Phanerochaete chrysosporium, catalyzes a key step in the degradation of vanillate, an intermediate in lignin degradation (25)....

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“…Catechol 1,2-dioxygenase (pyrocatechase I and II) was measured spectrofotometrically by the absorbency of the ortho cleavage product at A=260 nm, as described by Dorn & Knackmuss (1978). Before assaying catechol 1,2-dioxygenase, catechol 2,3-437 dioxygenase was destroyed by adding hydrogenperoxide, according to Nakazawa & Yokota (1973).…”

Section: Measurement Of Specific Activities Of Enzymes Involved In Bimentioning

confidence: 99%

“…Bacteria that efficiently degrade chlorobenzoates generally exhibit ortho cleavage of their chlorocatechols catalyzed by pyrocatechase II (Dorn & Knackmuss 1978). Alcaligenes sp.…”

Section: Introductionmentioning

confidence: 99%

Aerobic degradation of polychlorinated biphenyls by Alcaligenes sp. JB1: metabolites and enzymes

et al. 1997

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(1997). Aerobic degradation of polychlo-rinated biphenyls by Alcaligenes sp. JB1: metabolites and enzymes. Biodegradation, (7), 435-443. General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Key words: aerobic, biodegradation, enzymes, induction, polychlorinated biphenyls, resting-cell assay AbstractIn contrast to the degradation of penta-and hexachlorobiphenyls in chemostat cultures, the metabolism of PCBs by Alcaligenes sp. JB1 was shown to be restricted to PCBs with up to four chlorine substituents in resting-cell assays. Among these, the PCB congeners containing ortho chlorine substituents on both phenyl rings were found to be least degraded. Monochloro-benzoates and dichlorobenzoates were detected as metabolites. Resting cell assays with chlorobenzoates showed that JB1 could metabolize all three monochlorobenzoates and dichlorobenzoates containing only meta and para chlorine substituents, but not dichlorobenzoates possessing an ortho chlorine substituent. In enzyme activity assays, meta cleaving 2,3-dihydroxybiphenyl 1,2-dioxygenase and catechol 2,3-dioxygenase activities were constitutive, whereas benzoate dioxygenase and ortho cleaving catechol 1,2-dioxygenase activities were induced by their substrates. No activity was found for pyrocatechase II, the enzyme that is specific for chlorocatechots. The data suggest that complete mineralization of PCBs with three or more chlorine substituents byAlcaligenes sp. JB1 is unlikely.Abbreviations: PCB -polychlorinated biphenyls, CBA -chlorobenzoate, D -di-, Tr -tri-, Te -tetra-, Pe -penta-, H -hexa

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Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol

Cited by 331 publications

References 28 publications

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1

Aerobic degradation of polychlorinated biphenyls by Alcaligenes sp. JB1: metabolites and enzymes

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