Environmental and metabolic transformations of primary aromatic amines and related compounds

Parris, George E.

doi:10.1007/978-1-4612-6107-0_1

Cited by 62 publications

(47 citation statements)

References 80 publications

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“…The reduction intermediates, i.e., nitrosoaromatic, hydroxylaminoaromatic, and aminoaromatic compounds, easily form azo (24) and azoxy compounds (34), which are mostly end products of biotransformation. The capability to convert hydroxylaminobenzene to 2-aminophenol and to open the ring of 2-aminophenol with the ring fission enzyme described in this paper enables P. pseudoalcaligenes JS45 to avoid forming toxic end products and to use nitrobenzene as a source of carbon, nitrogen, and energy.…”

Section: Resultsmentioning

confidence: 99%

2-aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45

Lendenmann¹,

Spain²

1996

J Bacteriol

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Most bacterial pathways for the degradation of aromatic compounds involve introduction of two hydroxyl groups either ortho or para to each other. Ring fission then occurs at the bond adjacent to one of the hydroxyl groups. In contrast, 2-aminophenol is cleaved to 2-aminomuconic acid semialdehyde in the nitrobenzenedegrading strain Pseudomonas pseudoalcaligenes JS45. To examine the relationship between this enzyme and other dioxygenases, 2-aminophenol 1,6-dioxygenase has been purified by ethanol precipitation, gel filtration, and ion exchange chromatography. The molecular mass determined by gel filtration was 140,000 Da. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed two subunits of 35,000 and 39,000 Da, which suggested an ␣ 2 ␤ 2 subunit structure. Studies with inhibitors indicated that ferrous iron was the sole cofactor. The K m values for 2-aminophenol and oxygen were 4.2 and 710 M, respectively. The enzyme catalyzed the oxidation of catechol, 6-amino-m-cresol, 2-amino-m-cresol, and 2-amino-4-chlorophenol. 3-Hydroxyanthranilate, protocatechuate, gentisate, and 3-and 4-methylcatechol were not substrates. The substrate range and the subunit structure are unique among those of the known ring cleavage dioxygenases.Ring cleavage is a key reaction in microbial degradation of aromatic compounds. In aerobic bacteria, it is usually catalyzed by dioxygenases (17). Typically, substrates of ring cleavage dioxygenases feature an aromatic ring substituted with two hydroxyl groups oriented either ortho or para to each other (26). Indeed, nearly all bacterial catabolic pathways transform aromatic substrates to catechol or gentisate and their derivatives, which subsequently undergo ring cleavage (10).Recently, we reported the discovery of 2-aminophenol 1,6-dioxygenase, a new ring cleavage enzyme that catalyzes the direct conversion of 2-aminophenol to 2-aminomuconic acid semialdehyde. The enzyme is induced during the growth of Pseudomonas pseudoalcaligenes JS45 on nitrobenzene. The degradation pathway (Fig. 1A) starts with reduction of nitrobenzene to hydroxylaminobenzene followed by rearrangement to 2-aminophenol (19).Two enzymes have been reported to catalyze the ring cleavage of 2-aminophenol at very low rates. Catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 catalyzes extradiol ring fission of 2-aminophenol at a rate that is 0.1% that of the intradiol cleavage of catechol (27). 2-Aminophenol was oxidized by catechol 2,3-dioxygenase from P. arvilla at a rate less than 0.01% of the rate with catechol (14, 22). These low turnover rates indicate that 2-aminophenol is not a physiological substrate of catechol 1,2-or 2,3-dioxygenase. To our knowledge, this is the first report of an enzyme that cleaves 2-aminophenol as its primary substrate.We have purified and characterized 2-aminophenol 1,6-dioxygenase from P. pseudoalcaligenes JS45 to determine how it is related to previously known ring cleavage enzymes. The tertiary structure, substrate range, and cofactor requirement were compared with that of other ri...

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Section: Resultsmentioning

confidence: 99%

2-aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45

Lendenmann¹,

Spain²

1996

J Bacteriol

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“…This change reflects the accumulation of 4-chlorocatechol, as revealed by HPLC analysis, and suggests that further degradation of 4-chlorocatechol may be the rate-limiting step in the metabolism of 4CA by the bacterial consortium. In addition, it cannot be discounted that the dark brown colour was also the result of a non-enzymic conversion of aniline, 4-CA or 4-chlorocatechol to various oxidation products (Parris, 1980). For example, redox reactions can result in oxidative coupling of chloroanilines and chlorocatechols, whereas surface-catalysed reactions can result in aniline polymerization (Adriaens, 1997;Bachofer et al, 1975;Sjoblad & Bollag, 1981).…”

Section: Discussionmentioning

confidence: 99%

“…In this study unknown compounds were detected by HPLC-UV at retention times of 2?5 min and 5?5 min. It was possible that these unidentified compounds were transformation products from 4CA, non-enzymic oxidation products of 4-chlorocatechol (Parris, 1980), or modifications of 4CA to other chloroaromatic compounds. An example of the latter case was reported by Zeyer & Kearney (1982), who found 4,49-dichloroazobenzene in the culture filtrate of Moraxella sp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a soil-derived bacterial consortium degrading 4-chloroaniline

2003

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A bacterial consortium comprising four different species was isolated from an Indonesian agricultural soil using a mixture of aniline and 4-chloroaniline (4CA) as principal carbon sources. The four species were identified as Chryseobacterium indologenes SB1, Comamonas testosteroni SB2, Pseudomonas corrugata SB4 and Stenotrophomonas maltophilia SB5. Growth studies on aniline and 4CA as single and mixed substrates demonstrated that the bacteria preferred to grow on and utilize aniline rather than 4CA, although both compounds were eventually depleted from the culture supernatant. However, despite 100 % disappearance of the parent substrates, the degradation of 4CA was always characterized by incomplete dechlorination and 4-chlorocatechol accumulation. This result suggests that further degradation of 4-chlorocatechol may be the rate-limiting step in the metabolism of 4CA by the bacterial consortium. HPLC-UV analysis showed that 4-chlorocatechol was further degraded via an ortho-cleavage pathway by the bacterial consortium. This hypothesis was supported by the results from enzyme assays of the crude cell extract of the consortium revealing catechol 1,2-dioxygenase activity which converted catechol and 4-chlorocatechol to cis,cis-muconic acid and 3-chloro-cis,cis-muconic acid respectively. However, the enzyme had a much higher conversion rate for catechol [156 U (g protein)], indicating preference for non-chlorinated substrates. Members of the bacterial consortium were also characterized individually. All isolates were able to assimilate aniline. P. corrugata SB4 was able to grow on 4CA solely, while S. maltophilia SB5 was able to grow on 4-chlorocatechol. These results suggest that the degradation of 4CA in the presence of aniline by the bacterial consortium was a result of interspecies interactions.

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“…No changes were remarked in control flask. Conversion of DNB and AN to brown coloured oxygenated products was reported by Parris (1980). Polymerization of highly reactive catechol or protocatechute was reported also by Loidl et al (1990) and Bachofer et al (1975); it may give a reason for the accumulation of the brownish product.…”

Section: Degradation Of Dnb or An In Shaking Flasksmentioning

confidence: 86%

Bioremediation of 3,5-dinitrobenzoic acid and aniline by a Corynebacterium sp.

Ahmed¹,

Y²,

Kumosani³

et al. 2013

Afr. J. Microbiol. Res.

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Corynebacterium sp was isolated from the soil by using 3-5 dinitro benzoic acid (DNB) as a sole carbon source. The highest rate of degradation of aniline (AN) or DNB was found in the exponential phase of the growth of the bacterium. After 24 h, about 50% of DNB and 30% of AN were degraded by Corynebacterium sp. At a concentration of 0.5 to 1 g/L of AN or DNB, good growth was obtained and the protocatechuic acid was detected. The optimum concentration of yeast extract was 2 g/l. Catechol 1-2 dioxygenase was induced in the cells grown on a medium containing AN or DNB. A significant activity of this enzyme was detected, which means that ortho cleavage pathway may be present in Corynebacterium sp.

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Environmental and metabolic transformations of primary aromatic amines and related compounds

Cited by 62 publications

References 80 publications

2-aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45

2-aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45

Characterization of a soil-derived bacterial consortium degrading 4-chloroaniline

Bioremediation of 3,5-dinitrobenzoic acid and aniline by a Corynebacterium sp.

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