Microbial metabolism of aryl sulphonates A re-assessment of colorimetric methods for the determination of sulphite and their use in measuring desulphonation of aryl and alkylbenzene sulphonates

Johnston, James B.; Murray, Keith; Cain, Ronald B.

doi:10.1007/bf02565092

Cited by 58 publications

(47 citation statements)

References 22 publications

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“…oxygenation and hydrolysis. We detected a highly active, inducible sulfite dehydrogenase in cell extracts (see Johnston et al 1975;), and we presume that this enzyme activity explains why no sulfite is detected outside the cells during growth.…”

Section: Discussionmentioning

confidence: 68%

Ethanedisulfonate is degraded via sulfoacetaldehyde in Ralstonia sp. strain EDS1

Denger

Cook

2001

Archives of Microbiology

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Aerobic enrichment cultures (11) yielded three cultures able to utilise ethane-1,2-disulfonate as sole source of carbon and energy in salts medium. Two pure cultures were obtained and we worked with strain EDS1, which was assigned to the genus Ralstonia on the basis of its 16S rDNA sequence and simple taxonomic tests. Strain EDS1 utilised at least seven alkane(di)sulfonates, ethane-1,2-disulfonate, taurine, isethionate, sulfoacetate, sulfoacetaldehyde and propane-1,3-disulfonate, as well as methanesulfonate and formate. Growth with ethanedisulfonate was concomitant with substrate disappearance and the formation of 2 mol sulfate per mol substrate. The growth yield, 7 g protein (mol C) -1 , indicated quantitative utilisation of the substrate. Ethanedisulfonate-dependent oxygen uptake of whole cells during growth rose to a maximum before the end of growth and then sank rapidly; this was interpreted as evidence for an inducible desulfonative oxygenase that was not active in cell extracts. Inducible sulfoacetaldehyde sulfo-lyase was detected at high activity. Inducible degradation of taurine or isethionate or sulfoacetate via sulfoacetaldehyde sulfo-lyase is interpreted from the data.

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Section: Discussionmentioning

confidence: 68%

Ethanedisulfonate is degraded via sulfoacetaldehyde in Ralstonia sp. strain EDS1

Denger

Cook

2001

Archives of Microbiology

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“…Enzyme Assay-Taurine dioxygenase activity was assayed at 30°C by using Ellman's reagent (5,5Ј-dithiobis(2-nitrobenzoic acid)), which produces a bright yellow color upon reaction with sulfite (12,13). The assay mixture (1-ml final volume) contained 500 M taurine, 1 mM ␣-KG, 100 M Fe(II)SO 4 (freshly made), 200 M sodium ascorbate, and appropriate amounts of TauD in 10 mM imidazole buffer (pH 6.9).…”

Section: Methodsmentioning

confidence: 99%

Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

Eichhorn

Ploeg

Kertesz

et al. 1997

Journal of Biological Chemistry

250

288

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The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulfonic acid) as a sulfur source and is expressed only under conditions of sulfate starvation. The sequence relatedness of the TauD protein to the ␣-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase of Alcaligenes eutrophus suggested that TauD is an ␣-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulfite from taurine (van der Ploeg, J. R., Weiss, M. A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M. A., and Leisinger, T. (1996) J. Bacteriol. 178, 5438 -5446). TauD was overexpressed in E. coli to ϳ70% of the total soluble protein and purified to apparent homogeneity by a simple two-step procedure. The apparent M r of 81,000 of the native protein and the subunit M r of 37,400 were consistent with a homodimeric structure. The pure enzyme converted taurine to sulfite and aminoacetaldehyde, which was identified by high pressure liquid chromatography after enzymatic conversion to ethanolamine. The reaction also consumed equimolar amounts of oxygen and ␣-ketoglutarate; ferrous iron was absolutely required for activity; and ascorbate stimulated the reaction. The properties and amino acid sequence of this enzyme thus define it as a new member of the ␣-ketoglutarate-dependent dioxygenase family. The pure enzyme showed maximal activity at pH 6.9 and retained activity on storage at ؊20°C for several weeks. Taurine (K m ‫؍‬ 55 M) was the preferred substrate, but pentanesulfonic acid, 3-(N-morpholino)propanesulfonic acid, and 1,3-dioxo-2-isoindolineethanesulfonic acid were also desulfonated at significant rates. Among the cosubstrates tested, only ␣-ketoglutarate (K m ‫؍‬ 11 M) supported significant dioxygenase activity.In the absence of sulfate, Escherichia coli can utilize aliphatic sulfonates as sulfur sources for growth. Sulfonates known to provide sulfur include ethanesulfonate, butanesulfonate, L-cysteate, isethionate (2-hydroxyethanesulfonate), and taurine (2-aminoethanesulfonate) (1, 2). None of these sulfonates served as sulfur source under anaerobic conditions, nor could they be utilized as a source of carbon and energy or of carbon, energy, and sulfur under either aerobic or anaerobic conditions (1). The mechanisms of sulfur assimilation from aliphatic sulfonates are unknown, but it has been shown that sulfonate/sulfur enters the assimilatory sulfate reduction pathway at the stage of sulfite (3).Recently, we have identified the tauABCD gene cluster, located at 8.5 min on the E. coli chromosome, which is specifically involved in the utilization of taurine as a sulfur source (2). Disruption of tauB, tauC, or tauD resulted in the loss of the ability to utilize taurine as a source of sulfur, but did not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. The tau genes were only expressed during growth in the absence of sulfate or cysteine (2). The amino acid sequences of TauABC exhibit similarity to components of ABC-type transport systems (4). TauA has a p...

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“…The enzymatic release of sulfite from 4-sulfomuconolactone was quantified by using EllmanЈs reagent [5,5Ј-dithiobis(2-nitrobenzoic acid)] as described in the report by Johnston et al (21).…”

Section: Methodsmentioning

confidence: 99%

4-Sulfomuconolactone Hydrolases from Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2

et al. 2007

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The 4-carboxymethylen-4-sulfo-but-2-en-olide (4-sulfomuconolactone) hydrolases from Hydrogenophaga intermedia strain S1 and Agrobacterium radiobacter strain S2 are part of a modified protocatechuate pathway responsible for the degradation of 4-sulfocatechol. In both strains, the hydrolase-encoding genes occur downstream of those encoding the enzymes that catalyze the lactonization of 3-sulfomuconate. The deduced amino acid sequences of the 4-sulfomuconolactone hydrolases demonstrated the highest degree of sequence identity to 2-pyrone-4,6-dicarboxylate hydrolases, which take part in the meta cleavage pathway of protocatechuate. The 4-sulfomuconolactone hydrolases did not convert 2-pyrone-4,6-dicarboxylate, and the 2-pyrone-4,6-dicarboxylate hydrolase from Sphingomonas paucimobilis SYK-6 did not convert 4-sulfomuconolactone. Nevertheless, the presence of highly conserved histidine residues in the 4-sulfomuconolactone and the 2-pyrone-4,6-dicarboxylate hydrolases and some further sequence similarities suggested that both enzymes belong to the metallo-dependent hydrolases (the "amidohydrolase superfamily"). The 4-sulfomuconolactone hydrolases were heterologously expressed as His-tagged enzyme variants. Gel filtration experiments suggested that the enzymes are present as monomers in solution, with molecular weights of approximately 33,000 to 35,000. 4-Sulfomuconolactone was converted by sulfomuconolactone hydrolases to stoichiometric amounts of maleylacetate and sulfite. The 4-sulfomuconolactone hydrolases from both strains showed pH optima at pH 7 to 7.5 and rather similar catalytic constant (k cat /K M )values. The suggested 4-sulfocatechol pathway from 4-sulfocatechol to maleylacetate was confirmed by in situ nuclear magnetic resonance analysis using the recombinantly expressed enzymes.

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Microbial metabolism of aryl sulphonates A re-assessment of colorimetric methods for the determination of sulphite and their use in measuring desulphonation of aryl and alkylbenzene sulphonates

Cited by 58 publications

References 22 publications

Ethanedisulfonate is degraded via sulfoacetaldehyde in Ralstonia sp. strain EDS1

Ethanedisulfonate is degraded via sulfoacetaldehyde in Ralstonia sp. strain EDS1

Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

4-Sulfomuconolactone Hydrolases from Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2

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