The Role of Tetrathionate in the Oxidation of Thiosulphate by Chromatium sp. strain D

Smith, A. J.

doi:10.1099/00221287-42-3-371

Cited by 40 publications

(15 citation statements)

References 13 publications

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“…A thiosulphate dehydrogenase is responsible for the oxidation to tetrathionate, while a sox gene‐encoded multienzyme complex is essential for the oxidation to sulphate. In conjunction with its localization in the bacterial periplasm, the low pH optimum of 4.25 for the A. vinosum thiosulphate dehydrogenase is in full agreement with the observation that whole cells preferably form tetrathionate from thiosulphate at pH values below 7.0 while sulphate is the main product under alkaline conditions (Smith, 1966; Smith and Lascelles, 1966).…”

Section: Discussionsupporting

confidence: 84%

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Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Hensen

Sperling

Trüper

et al. 2006

Molecular Microbiology

167

192

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SummaryTwo different pathways for thiosulphate oxidation are present in the purple sulphur bacterium Allochromatium vinosum: oxidation to tetrathionate and complete oxidation to sulphate with obligatory formation of sulphur globules as intermediates. The tetrathionate:sulphate ratio is strongly pH-dependent with tetrathionate formation being preferred under acidic conditions. Thiosulphate dehydrogenase, a constitutively expressed monomeric 30 kDa c-type cytochrome with a pH optimum at pH 4.2 catalyses tetrathionate formation. A periplasmic thiosulphateoxidizing multienzyme complex (Sox) has been described to be responsible for formation of sulphate from thiosulphate in chemotrophic and phototrophic sulphur oxidizers that do not form sulphur deposits. In the sulphur-storing A. vinosum we identified five sox genes in two independent loci (soxBXA and soxYZ). For SoxA a thiosulphate-dependent induction of expression, above a low constitutive level, was observed. Three sox-encoded proteins were purified: the heterodimeric c-type cytochrome SoxXA, the monomeric SoxB and the heterodimeric SoxYZ. Gene inactivation and complementation experiments proved these proteins to be indispensable for thiosulphate oxidation to sulphate. The intermediary formation of sulphur globules in A. vinosum appears to be related to the lack of soxCD genes, the products of which are proposed to oxidize SoxY-bound sulphane sulphur. In their absence the latter is instead transferred to growing sulphur globules.

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Section: Discussionsupporting

confidence: 84%

“…The properties of thiosulphate dehydrogenase from A. vinosum characterized during this study are compatible with older data presented by Smith (1966) and Fukumori and Yamanaka (1979). In both reports a tetrathionateforming activity with a pH optimum in the acidic range was described.…”

Section: Tetrathionate-forming Thiosulphate Dehydrogenase Is An Acidosupporting

confidence: 93%

Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Hensen

Sperling

Trüper

et al. 2006

Molecular Microbiology

167

192

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“…3a). As expected for C. vinostlm at neutral to slightly acidic pH (Smith, 1966), both wild-type and mutant strain oxidized thiosulphate partly to sulphate with an intermediary formation of intracellular sulphur and partly to tetrathionate, which was not further metabolized ( Fig. 3c, d).…”

Section: Biochemical and Physiological Characterization Of Mutant Strmentioning

confidence: 84%

Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum

Dahl

1996

Microbiology

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In purple sulphur bacteria of the family Chmmatiaceae sulphite oxidation via intermediary formation of adenylylsulphate is an enzymologically well characterized process. In contrast, the role of an alternative direct oxidation pathway via the enzyme su1phite:acceptor oxidoreductase has not been resolved. This paper reports the cloning of the genes encoding the adenylylsulphate-forming enzyme adenosine-5'-phosphosulphate (APS) reductase from Chromatium winosum strain D (DSM 1803, a representative of the purple sulphur bacteria, and the construction of mutations in these genes by insertion of a kanamycin cartridge. The mutated genes were transferred to C. winosum on suicide vectors of the pSUP series by conjugation and delivered to the chromosome by double homologous recombination. Southern hybridization and PCR analyses of the recombinants obtained verified the first insertional gene inactivation in purple sulphur bacteria. Enzymological studies demonstrated the absence of APS reductase from the mutants. Further phenotypic characterization showed no significant effect of APS reductase deficiency on the sulphite-oxidizing ability of the cells under photolithoautotrophic growth conditions. In the wild-type as well as in mutant strains, tungstate, the specific antagonist of molybdate, led to the intermediary accumulation of sulphite in the medium during sulphide oxidation and strongly inhibited growth with sulphite as photosynthetic electron donor; this indicates that a molybdoenzyme, probably su1phite:acceptor oxidoreductase, is the main sulphite-oxidizing enzyme in C. winosum. Specific inactivation of selected genes as developed for C. winosum in this study provides a powerful genetic tool for further analysis of sulphur metabolism and other metabolic pathways in phototrophic sulphur bacteria.

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“…vinosum (Smith 1966;Smith and Lascelles 1966;Hashwa 1975;Fukumori and Yamanaka 1979b), alternate sulfide-oxidizing systems have been heretofore unknown. We readily detected sulfide:quinone oxidoreductase activity in crude extracts of the wild-type and mutant FD1, and suggest that sulfide oxidation in Chr.…”

Section: Discussionmentioning

confidence: 99%

“…As expected for Chr. vinosum during photolithoautotrophic growth at neutral to slightly acidic pH (Smith 1966), the wild-type and the mutant oxidized thiosulfate (1.5 mM) partly to tetrathionate and partly to sulfate when grown in batch culture at pH 7 (not shown). The ratio of tetrathionate/sulfate formed did not differ significantly in both strains and was in the same range as observed earlier for Chr.…”

Section: Strainmentioning

confidence: 91%

Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum

Reinartz

Tschäpe²,

Brüser³

et al. 1998

Archives of Microbiology

118

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Sulfide oxidation in the phototrophic purple sulfur bacterium Chromatium vinosum D (DSMZ 180(T)) was studied by insertional inactivation of the fccAB genes, which encode flavocytochrome c, a protein that exhibits sulfide dehydrogenase activity in vitro. Flavocytochrome c is located in the periplasmic space as shown by a PhoA fusion to the signal peptide of the hemoprotein subunit. The genotype of the flavocytochrome-c-deficient Chr. vinosum strain FD1 was verified by Southern hybridization and PCR, and the absence of flavocytochrome c in the mutant was proven at the protein level. The oxidation of thiosulfate and intracellular sulfur by the flavocytochrome-c-deficient mutant was comparable to that of the wild-type. Disruption of the fccAB genes did not have any significant effect on the sulfide-oxidizing ability of the cells, showing that flavocytochrome c is not essential for oxidation of sulfide to intracellular sulfur and indicating the presence of a distinct sulfide-oxidizing system. In accordance with these results, Chr. vinosum extracts catalyzed electron transfer from sulfide to externally added duroquinone, indicating the presence of the enzyme sulfide:quinone oxidoreductase (EC 1.8.5.-). Further investigations showed that the sulfide:quinone oxidoreductase activity was sensitive to heat and to quinone analogue inhibitors. The enzyme is strictly membrane-bound and is constitutively expressed. The presence of sulfide:quinone oxidoreductase points to a connection of sulfide oxidation to the membrane electron transport system at the level of the quinone pool in Chr. vinosum.

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The Role of Tetrathionate in the Oxidation of Thiosulphate by Chromatium sp. strain D

Cited by 40 publications

References 13 publications

Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum

Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum

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