Pigments of pseudomonas species. Part III. The synthesis of demethylaeruginosin B and aeruginosin B

Bentley, R. K.; Holliman, F. G.

doi:10.1039/j39700002447

Cited by 8 publications

(5 citation statements)

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“…267 (Budzikiewicz et al 1998), pseudoalterobactin A and B produced by Pseudoalteromonas sp. KP20-4 (Kanoh et al 2003), aeruginosin B produced by Pseudomonas aeruginosa (Herbert and Holliman 1969); (Bentley and Holliman 1970), as well as petrobactin sulfonate produced by M. hydrocarbonoclasticus (Hickford et al 2004). Except for aeruginosin B, the sulfonate group in the natural products mentioned above, is found adjacent to a hydroxyl group.…”

Section: Discussionmentioning

confidence: 99%

Siderophores of Marinobacter aquaeolei: petrobactin and its sulfonated derivatives

et al. 2009

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Siderophores are low molecular weight, high-affinity iron(III) ligands, produced by bacteria to solubilize and promote iron uptake under low iron conditions. Two prominent structural features characterize the majority of the marine siderophores discovered so far: (1) a predominance of suites of amphiphilic siderophores composed of an iron(III)-binding headgroup that is appended by one or two of a series of fatty acids and (2) a prevalence of siderophores that contain α-hydroxycarboxylic acid moieties (e.g., β-hydroxyaspartic acid or citric acid) which are photoreactive when coordinated to Fe(III). Variation of the fatty acid chain length affects the relative amphiphilicity within a suite of siderophores. Catecholate sulfonation is another structural variation that would affect the hydrophilicity of a siderophore. In addition to a review of the marine amphiphilic siderophores, we report the production of petrobactin disulfonate by Marinobacter aquaeolei VT8.

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Section: Discussionmentioning

confidence: 99%

Siderophores of Marinobacter aquaeolei: petrobactin and its sulfonated derivatives

et al. 2009

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“…An unde¢ned, but presumably aliphatic compound is found in high concentrations in plasma cells from heart samples of Ascidia ceratodes [23]. In contrast to these aliphatic compounds, only one de¢ned aromatic sulfonate seems to be known, aeruginosin B [169]. Unde¢ned sulfonates in soils, largely in humic materials, and in marine sediments seem to be widespread [25 27].…”

Section: Xenobiotic Sulfonates In the Environmentmentioning

confidence: 99%

Microbial desulfonation

Cook

1998

FEMS Microbiology Reviews

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Organosulfonates are widespread compounds, be they natural products of low or high molecular weight, or xenobiotics. Many commonly found compounds are subject to desulfonation, even if it is not certain whether all the corresponding enzymes are widely expressed in nature. Sulfonates require transport systems to cross the cell membrane, but few physiological data and no biochemical data on this topic are available, though the sequences of some of the appropriate genes are known. Desulfonative enzymes in aerobic bacteria are generally regulated by induction, if the sulfonate is serving as a carbon and energy source, or by a global network for sulfur scavenging (sulfate starvation induced (SSI) stimulon) if the sulfonate is serving as a source of sulfur. It is unclear whether an SSI regulation is found in anaerobes. The anaerobic bacteria examined can express the degradative enzymes constitutively, if the sulfonate is being utilized as a carbon source, but enzyme induction has also been observed. At least three general mechanisms of desulfonation are recognisable or postulated in the aerobic catabolism of sulfonates: (1) activate the carbon neighboring the C y Q bond and release of sulfite assisted by a thiamine pyrophosphate cofactor; (2) destabilize the C y Q bond by addition of an oxygen atom to the same carbon, usually directly by oxygenation, and loss of the good leaving group, sulfite; (3) an unidentified, formally reductive reaction. Under SSIS control, different variants of mechanism (2) can be seen. Catabolism of sulfonates by anaerobes was discovered recently, and the degradation of taurine involves mechanism (1). When anaerobes assimilate sulfonate sulfur, there is one common, unknown mechanism to desulfonate the inert aromatic compounds and another to desulfonate inert aliphatic compounds; taurine seems to be desulfonated by mechanism (1).

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“…We used to presume that the degradation of sulfobenzoate was more recent, given that only one naturally occurring aromatic sulfonate of low molecular mass was known (Bentley & Holliman, 1970). Now it is clear that a natural sulfonated polymer (humic acid) is widespread (van Loon e t al., 1993) and likely, based on its low pK value, to contain sulfonated benzene rings, so it is possible that the degradation of sulfobenzoate is also ancient.…”

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confidence: 99%

Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2

et al. 1996

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Three multicomponent oxygenases involved in the degradation of ptoluenesulfonate and p-toluenecarboxylate and the regulation o f their synthesis have been examined in three strains (T-2, PSB-4 and TER-1) of Cornamonas testosteroni. Strain T-2 utilizes p-toluenesulfonate as a source of carbon and energy for growth via p-sulfobenzoate and protocatechuate, and ptoluenecarboxylate via terephthalate and protocatechuate, and ha5 the unusual property of requiring the reductase (TsaE) of the toluenesulfonate methyl monooxygenase system (TsaMB) in an incompletely expressed sulfobenzoate dioxygenase system (PsbAC) [Schlafli Oppenberg, H. R. , Chen, G., terephthalate via protoeateehuate. Mutant TER-1, derived from strain T-2, utilized only terephthalate via protocatechuate. We detected no enzymes of the pathway from toluenesulfonate to sulfobenzoate in strains PSB-4 and TER-I , and Confirmed by PCR and Southern blot analysis that the genes (tsaMB) encoding toluenesulfonate monooxygenase were absent. We concluded that, in strain PSB-4, the regulatory unit encoding the genes for the conversion of toluenesulfonate to sulfobenzoate was missing. and that generation of mutant TER-1 involved deletion of this regulatory unit and of the regulatory unit encoding desulfonation of sulfobenzoate. The degradation of sulfobenzoate in strain PSB-4 was catalysed by a fully inducible sulfobenzoate dioxygenase system ( PsbAC, , , , ) , which, after purification of the oxygenase component (PsbA,,), turned out to be indistinguishable from the corresponding component from strain T-2 (PsbA, , ).Reductase P s b C , , , . which w e could separate but not purify, was active with oxygenase PsbA, , , , and Psbh-,. Oxygenase P s b A , , , was shown by electron paramagnetic resonance spectroscopy to contain a Rieske [2Fe-2S] centre. The enzyme system oxygenating terephthalate was examined and the oxygenasc component purified and characterized. The oxygenase component in strains T-2 (and mutant TER-I) and PSB-4 were indistinguishable. The reductase component, which w e separated but failed to purify, was active with the oxygenase from all strains. Gains and losses of blocks of genes in evolution is discussed.

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Pigments of pseudomonas species. Part III. The synthesis of demethylaeruginosin B and aeruginosin B

Cited by 8 publications

References 0 publications

Siderophores of Marinobacter aquaeolei: petrobactin and its sulfonated derivatives

Siderophores of Marinobacter aquaeolei: petrobactin and its sulfonated derivatives

Microbial desulfonation

Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2

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