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- W2061878641 abstract "ABSTRACT Thiosulfate respiration in Salmonella enterica serovar Typhimurium is catalyzed by the membrane-bound enzyme thiosulfate reductase. Experiments with quinone biosynthesis mutants show that menaquinol is the sole electron donor to thiosulfate reductase. However, the reduction of thiosulfate by menaquinol is highly endergonic under standard conditions (Δ E °′ = −328 mV). Thiosulfate reductase activity was found to depend on the proton motive force (PMF) across the cytoplasmic membrane. A structural model for thiosulfate reductase suggests that the PMF drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase was 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 was PMF independent. Electron transfer from formate to thiosulfate in whole cells occurs predominantly by intraspecies hydrogen transfer." @default.
- W2061878641 created "2016-06-24" @default.
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- W2061878641 creator A5088245799 @default.
- W2061878641 creator A5089137986 @default.
- W2061878641 date "2012-01-15" @default.
- W2061878641 modified "2023-09-30" @default.
- W2061878641 title "Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force" @default.
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- W2061878641 doi "https://doi.org/10.1128/jb.06014-11" @default.
- W2061878641 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3256639" @default.
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