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Literature summary for 1.8.5.5 extracted from

  • Stoffels, L.; Krehenbrink, M.; Berks, B.C.; Unden, G.
    Thiosulfate reduction in Salmonella enterica is driven by the proton motive force (2012), J. Bacteriol., 194, 475-485.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Salmonella enterica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfite + hydrogen sulfide + menaquinone
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Salmonella enterica thiosulfate + menaquinol thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction r
thiosulfate + menaquinol
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Salmonella enterica sulfite + hydrogen sulfide + menaquinone
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r

Cofactor

Cofactor Comment Organism Structure
menaquinol menaquinol is the sole electron donor to thiosulfate reductase Salmonella enterica

General Information

General Information Comment Organism
physiological function thiosulfate reductase activity depends on the proton motive force across the cytoplasmic membrane. The proton motive force drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase is able to catalyze the combined oxidation of sulfide and sulfite to thiosulfate in a reverse of the physiological reaction. In contrast to the forward reaction, the exergonic thiosulfate-forming reaction is independent of the proton motive force Salmonella enterica