Novel Partial Reductive Pathway for 4-Chloronitrobenzene and Nitrobenzene Degradation in<i>Comamonas</i>sp. Strain CNB-1

Wu, Jianfeng; Jiang, Cheng‐Ying; Wang, Baojun; Ma, Yingfei; Liu, Zhi-Pei; Liu, Shuang‐Jiang

doi:10.1128/aem.72.3.1759-1765.2006

Cited by 143 publications

(101 citation statements)

References 41 publications

(19 reference statements)

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“…During partial reduction, as illustrated in Pseudomonas pseudoalcaligenes JS45, nitrobenzene is reduced through nitrosobenzene to hydroxylaminobenzene (25). Similar partial reductive metabolism was also observed for the degradation of other nitroaromatics, such as MNP (30), nitrobenzene (28), and chlorinated nitrobenzene (40,41). In the oxidative pathway, however, the nitro groups are directly removed from the aromatic ring with concomitant nitrite release, catalyzed by nitroarene dioxygenases or monooxygenases.…”

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confidence: 83%

Molecular Characterization of a Novel ortho -Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215

et al. 2007

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Alcaligenes sp. strain NyZ215 was isolated for its ability to grow on ortho-nitrophenol (ONP) as the sole source of carbon, nitrogen, and energy and was shown to degrade ONP via a catechol ortho-cleavage pathway. A 10,152-bp DNA fragment extending from a conserved region of the catechol 1,2-dioxygenase gene was obtained by genome walking. Of seven complete open reading frames deduced from this fragment, three (onpABC) have been shown to encode the enzymes involved in the initial reactions of ONP catabolism in this strain. OnpA, which shares 26% identity with salicylate 1-monooxygenase of Pseudomonas stutzeri AN10, is an ONP 2-monooxygenase (EC 1.14.13.31) which converts ONP to catechol in the presence of NADPH, with concomitant nitrite release. OnpC is a catechol 1,2-dioxygenase catalyzing the oxidation of catechol to cis,cismuconic acid. OnpB exhibits 54% identity with the reductase subunit of vanillate O-demethylase in Pseudomonas fluorescens BF13. OnpAB (but not OnpA alone) conferred on the catechol utilizer Pseudomonas putida PaW340 the ability to grow on ONP. This suggests that OnpB may also be involved in ONP degradation in vivo as an o-benzoquinone reductase converting o-benzoquinone to catechol. This is analogous to the reduction of tetrachlorobenzoquinone to tetrachlorohydroquinone by a tetrachlorobenzoquinone reductase (PcpD, 38% identity with OnpB) in the pentachlorophenol degrader Sphingobium chlorophenolicum ATCC 39723.

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confidence: 83%

Molecular Characterization of a Novel ortho -Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215

et al. 2007

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“…17A). Ring cleavage by 2-aminophenol 1,6-dioxygenase produces 2-amino-5-chloromuconate, which is converted to TCA cycle intermediates after additional enzymatic steps (209). Recently, mutant forms of nitrobenzene dioxygenase from Comamonas sp.…”

Section: Pathways For Chloronitrobenzene Catabolismmentioning

confidence: 99%

“…Comamonas sp. strain CNB-1 uses a pathway similar to that in JS45 for growth on both nitrobenzene and 4-chloronitrobenzene (209).…”

Section: Pathways For Nitrobenzene Catabolismmentioning

confidence: 99%

“…Comamonas sp. strain CNB-1 (209), Pseudomonas putida ZWL73 (219), and Comamonas sp. strain LW1 (94) each use a nitroreductase to reduce 4-chloronitrobenzene to 1-chloro-4-hydroxylaminobenzene, which is further transformed to 2-amino-5-chlorophenol by a hydroxylaminobenzene mutase or via Bamberger rearrangement (Fig.…”

Section: Pathways For Chloronitrobenzene Catabolismmentioning

confidence: 99%

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Nitroaromatic Compounds, from Synthesis to Biodegradation

Parales

2010

Microbiol Mol Biol Rev

707

453

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SUMMARY Nitroaromatic compounds are relatively rare in nature and have been introduced into the environment mainly by human activities. This important class of industrial chemicals is widely used in the synthesis of many diverse products, including dyes, polymers, pesticides, and explosives. Unfortunately, their extensive use has led to environmental contamination of soil and groundwater. The nitro group, which provides chemical and functional diversity in these molecules, also contributes to the recalcitrance of these compounds to biodegradation. The electron-withdrawing nature of the nitro group, in concert with the stability of the benzene ring, makes nitroaromatic compounds resistant to oxidative degradation. Recalcitrance is further compounded by their acute toxicity, mutagenicity, and easy reduction into carcinogenic aromatic amines. Nitroaromatic compounds are hazardous to human health and are registered on the U.S. Environmental Protection Agency's list of priority pollutants for environmental remediation. Although the majority of these compounds are synthetic in nature, microorganisms in contaminated environments have rapidly adapted to their presence by evolving new biodegradation pathways that take advantage of them as sources of carbon, nitrogen, and energy. This review provides an overview of the synthesis of both man-made and biogenic nitroaromatic compounds, the bacteria that have been identified to grow on and completely mineralize nitroaromatic compounds, and the pathways that are present in these strains. The possible evolutionary origins of the newly evolved pathways are also discussed.

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“…2-Amino-5-chloromuconate is an intermediate in the 4-CNB degradation pathway of Comamonas sp. strain CNB-1 (21). cnbH occurs in the degradative cnb cluster and encodes 2-amino-5-chloromuconate deaminase (21).…”

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A Novel Deaminase Involved in Chloronitrobenzene and Nitrobenzene Degradation with Comamonas sp. Strain CNB-1

Liu

et al. 2007

J Bacteriol

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Comamonas sp. strain CNB-1 degrades nitrobenzene and chloronitrobenzene via the intermediates 2-aminomuconate and 2-amino-5-chloromuconate, respectively. Deamination of these two compounds results in the release of ammonia, which is used as a source of nitrogen for bacterial growth. In this study, a novel deaminase was purified from Comamonas strain CNB-1, and the gene (cnbZ) encoding this enzyme was cloned. The N-terminal sequence and peptide fingerprints of this deaminase were determined, and BLAST searches revealed no match with significant similarity to any functionally characterized proteins. The purified deaminase is a monomer (30 kDa), and its V max values for 2-aminomuconate and 2-amino-5-chloromuconate were 147 mol ⅐ min ؊1 ⅐ mg ؊1 and 196 mol ⅐ min ؊1 ⅐ mg ؊1 , respectively. Its catalytic products from 2-aminomuconate and 2-amino-5-chloromuconate were 2-hydroxymuconate and 2-hydroxy-5-chloromuconate, respectively, which are different from those previously reported for the deaminases of Pseudomonas species. In the catalytic mechanism proposed, the ␣-carbon and nitrogen atoms (of both 2-aminomuconate and 2-amino-5-chloromuconate) were simultaneously attacked by a hydroxyl group and a proton, respectively. Homologs of cnbZ were identified in the genomes of Bradyrhizobium japonicum, Rhodopseudomonas palustris, and Roseiflexus sp. strain RS-1; these genes were previously annotated as encoding hypothetical proteins of unknown function. It is concluded that CnbZ represents a novel enzyme that deaminates xenobiotic compounds and/or ␣-amino acids.2-Aminomuconate deaminase (2-aminomuconate aminohydrolase; EC 3.5.99.5) converts 2-aminomuconate to 4-oxalocrotonate (2-hydroxymuconate) and ammonia. It is involved in biodegradation of natural compounds, such as tryptophan (4), as well as xenobiotic compounds, such as nitrobenzene (6, 7), aminophenol (17), and 2-nitrobenzoate (11). 2-Aminomuconate deaminases have been identified in several Pseudomonas strains (17) and Burkholderia cepacia (4). A new type of deaminase has recently been discovered in Bordetella sp. strain 10d that is highly specific for 2-amino-5-carboxymuconic 6-semialdehyde; 2-aminomuconate is not deaminated (12). Neither the nucleotide nor amino acid sequence of this deaminase has been reported.Certain bacteria or microbial consortia can utilize 4-chloronitrobenzene (4-CNB) as the sole source of carbon and nitrogen (9, 14, 22). 2-Amino-5-chloromuconate is an intermediate in the 4-CNB degradation pathway of Comamonas sp. strain CNB-1 (21). cnbH occurs in the degradative cnb cluster and encodes 2-amino-5-chloromuconate deaminase (21). However, the specific activity of CnbH expressed in Escherichia coli is 7 nmol min Ϫ1 (mg of cellular protein) Ϫ1 (2-aminomuconate as the substrate) (21), an activity that would appear to be too inefficient for bacterial growth. Indeed, the deaminase activity of cellular lysates of Comamonas sp. strain CNB-1 approximates 2.5 mol min Ϫ1 (mg of cellular protein Ϫ1 ) (2-aminomuconate as the substrate) (unpublished data). The...

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Novel Partial Reductive Pathway for 4-Chloronitrobenzene and Nitrobenzene Degradation inComamonassp. Strain CNB-1

Cited by 143 publications

References 41 publications

Molecular Characterization of a Novel ortho -Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215

Molecular Characterization of a Novel ortho -Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215

Nitroaromatic Compounds, from Synthesis to Biodegradation

A Novel Deaminase Involved in Chloronitrobenzene and Nitrobenzene Degradation with Comamonas sp. Strain CNB-1

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