The origin of the oxygen incorporated during the dehalogenation/hydroxylation of 4-chlorobenzoate by an Arthrobacter sp

Marks, Trevor S.; Wait, Robin; Smith, Andrew; Quirk, Alan V.

doi:10.1016/0006-291x(84)91607-3

Cited by 53 publications

(28 citation statements)

References 8 publications

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“…The enzymes which have been observed to catalyze the dehalogenation of chlorinated aromatic compounds (18,23) have not been purified. On the basis of substrate specificity, the dehalogenase of strain m15-3 is different from those enzymes.…”

Section: Resultsmentioning

confidence: 99%

Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3

Yokota¹,

Omori²,

Kodama³

1987

J Bacteriol

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A haloalkane dehalogenase was purified to electrophoretic homogeneity from cell extracts of a 1-chlorobutane-utiizing strain, m15-3, which was identified as a Corynebacterium sp. The enzyme hydrolyzed C2 to C12 mono-and dihalogenated alkanes, some haloalcohols, and haloacids. The K,,, value of the enzyme for 1-chlorobutane was 0.18 mM. Its molecular weight was estimated to be 36,000 by sodium dodecyl sulfatepolyacrylamide gel electrophoresis and 33,000 by gel filtration. The isoelectric point was pH 4.5. The optimum pH for enzyme activity was found to be 9.4, and the optimum temperature was 30 to 35°C. The enzyme was stable for 1 h at temperatures ranging from 4 to 30°C but was progressively less stable at 40 and 50°C.1-Chlorobutane-utilizing bacteria, Cornybacterium sp. strains tn2C-32 and m15-3, are able to grow with 1-chlorobutane as the sole carbon and energy source. Strain m2C-32 dehalogenated a variety of halogenated compounds, such as 1-chlorobutane, 1,9-dichlorononane, 4-chlorobutanol, and 3-chloropropionic acid, under aerobic conditions; however, under anaerobic conditions the strain dehalogenated only haloalkanes. Those halogenated compounds, except for haloacids, were dehalogenated by the cell extract of strain m2C-32. The cell extract, having a broad substrate specificity, dehalogenated C2 to Cg haloalkanes to produce alcohols (33).Two kinds of haloacid dehalogenases, haloacetate, dehalogenase (EC 3.8.1.3) (8, 13, 14, 28) and 2-haloacid dehalogenase (EC 3.8.1.2) (9, 17, 21), have been found. Furthermore, a DL-2-haloacid dehalogenase was purified from a Pseudomonas sp. (22). A number of dehalogenases which are active with haloacids have been purified and characterized, whereas only two enzymes which dehalogenate short-carbon-chain haloalkanes have been demonstrated. A. glutathione-dependent dehalogenase which acts on dihalomethanes was purified from Hyphomicrobium sp. strain DM2 (16), and a haloalkane dehalogenase which catalyzed hydrolytic dehalogenation of n-halogenated C1 to C4 alkanes was purified from Xanthobacter autotrophicus GJ10 (15). The dehalogenase of X. autotrophicus GJ10 was found to be constitutively produced (12), and the dehalogenases of 1-chlorobutane-utilizing strains m2C-32 and m15-3 were found to be inducible. The substrate specificities of all of the dehalogenases which have ever been purified were rather narrow, whereas the dehalogenase of strain m2C-32 seemed to have a very wide range of substrate specificity. However, we could not purify the dehalogenase of strain m2C-32 to homogeneity. On the other hand, the resting cells and cell extract of strain m15-3 also showed almost the sam.e substrate specificity as did those of strain m2C-32, Which suggested the presence of a haloalkane dehalQgenase with a broad substrate specificity in the cell extract of straih m15-3. Therefore, in this paper we describe the purification and properties of a haloalkane dehalogenase from the 1-chlorobutane-utilizing bacterium strain m15-3. * Corresponding author. MATERIALS AND METHODSMaterials. DEAE-...

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Section: Resultsmentioning

confidence: 99%

Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3

Yokota¹,

Omori²,

Kodama³

1987

J Bacteriol

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“…Different concentrations for 3,4-DCBA were monitored by measuring the maximum absorbance at (230 nm) using (UV/VIS spectrometer perkinelmer lambda 25). The supernatant was diluted 10 times (Marks et al, 1984) and in order to measure inorganic chloride was determined turbid metrically by measuring AgCl precipitation. Samples (1 ml) were acidified with (10 µl) of 10 NH 2 SO 4 and centrifuged at 14.000 rpm for 5 min to remove material that precipitated due to acidification alone.…”

Section: Determination Of Growth Degradation and Chloride Productionmentioning

confidence: 99%

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Alqudah¹,

Tarawneh²,

Alkafaween³

et al. 2014

IJB

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Chlorinated benzoic acids (CBA) have been intentionally released to the environment due to their use in agriculture as herbicides or pesticides, or unintentionally because they are common metabolites in the aerobic transformation of many chlorinated pollutants. The biodegradation of 3,4-dichlorobenzoic acid compound was investigated by using Corynebacterium jeikeium bacteria, which was isolated from Petra wastewater plant in Jordan. 3,4-dichlorobenzoic acid compound (3,4-DCBA) was used as a sole carbon and energy source in minimal salt media (MSM). 3,4-DCBA was the most degradable compound among the Chlorobenzoic acid compounds tested by this bacteria. Different conditions such as substrate concentration, temperature, pH, agitation rate, carbon starvation and carbon adaptation were used to obtain optimal Biodegradation. The optimal conditions for the biodegradation were 3mM as substrate concentration and the culture conditions were also showed a significant impact on the ability of these cells to remove 3,4-DCBA. The optimum solution, temperature and agitation rate were 7.5, 37 °C and 150 rpm, respectively. Adaptation of the cells to 3,4-DCBA for 24 hr and 48 hr and cells starvation for 24 hr and 48 hr increased the initial degradation rate. The degradation ability was monitored through disappearance of the substrate from the medium and the measuring the accompanying chloride release. Corynebacterium jeikeium dioxygenases were physiologically induced by 3,4-DCBA compound. They were analyzed for both ortho or meta ring-cleavage of this aromatic compound. Only 1,2-dioxygenase activity was detected which mean that the cleavage is through the ortho pathway. This microorganism can be a valuable and promising candidate for use in the biotreatment of wastewater samples contaminated with 3,4-DCBA.

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“…According to the numerous studies on microbial degradation of halogenated compounds, both strategies-initial dehalogenation and dehalogenation in a later stage of substrate catabolism-exist. Anaerobic degradation sequences of halogenated aromatics (7,36) as well as aliphatic compounds (8) (25,29), whereas mutants derived from Pseudomonas sp. strain B13 metabolize 3-chlorobenzoate and 4-chlorobenzoate to chlorinated cis-,cis-muconates, which are subsequently subjected to enzymatic dechlorination (30).…”

Section: Discussionmentioning

confidence: 99%

Microbial degradation of beta-chlorinated four-carbon aliphatic acids

Kohler-Staub

Köhler

1989

J Bacteriol

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Alcaligenes sp. strain CC1 is able to grow on several a-chlorinated aliphatic acids (2-chlorobutyrate, 2-chloropropionate, and chloroacetate), as wel as on the n-chlorinated four-carbon aliphatic acids trans-3-chlorocrotonate, cis-3-chlorocrotonate, and 3-chlorobutyrate as sole carbon and energy sources. Dehalogenation of a-chlorinated acids could be measured by using resting cells grown on all the different carbon sources, whereas dehalogenation of P-chlorinated four-carbon acids could be detected only by using resting ceUls grown on four-carbon compounds. A constitutive 2-haloacid dehalogenase, which did not show any activity with ,8-chlorinated four-arbon acids, was detected in cell extracts. Cell extracts of crotonate-grown cells additionally contained a 1-haloacid dechlorination activity, which acted on trans-3-chlorocrotonate, cis-3-chlorocrotonate, and 3-chlorobutyrate and was strictly dependent on coenzyme A, ATP, and Mge.Dechlorination of 13-chlorinated four-carbon acids takes place after activation of the acids to their coenzyme A derivatives and seems to be independent of the constitutive 2-haloacid dehalogenase.

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The origin of the oxygen incorporated during the dehalogenation/hydroxylation of 4-chlorobenzoate by an Arthrobacter sp

Cited by 53 publications

References 8 publications

Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3

Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Microbial degradation of beta-chlorinated four-carbon aliphatic acids

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