0000000000673739

AUTHOR

Martin Krehenbrink

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Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force

2012

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 …

ThiosulfatesSulfurtransferaseElectron donorNaphtholsBiologyPhotochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundElectron transferSulfiteEscherichia coliFormateMolecular BiologyExergonic reactionThiosulfateTerpenesChemiosmosisProton-Motive ForceSalmonella entericaGene Expression Regulation BacterialArticleschemistryBiochemistrySulfurtransferasesThermodynamicsProtonsOxidation-ReductionJournal of Bacteriology
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