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Results 1 - 4 of 4
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General Information
Commentary
Reference
physiological function
gene cluster phsBCDEF is essential for the anaerobic production of hydrogen sulfide from thiosulfate. Five potential translationally coupled open reading frames are present. Their putative protein products constitute a membrane-associated electron transport chain which contains proteins potentially capable of ligating iron-sulfur clusters and heme
physiological function
mutants defective in phs and chlA also lack a methyl viologen-linked thiosulfate reductase activity present in anaerobically grown wild-type cultures. Temperature-sensitive phs mutants produce H2S and methyl viologen-linked thiosulfate reductase at 30°C but not at 42°C. The reductases in all such mutants grown at 30°C are as thermostable as the wild-type enzyme and do not differ in electrophoretic relative mobility. The phs gene may encode a regulatory protein essential for the reduction of thiosulfate to hydrogen sulfide
physiological function
the Phs chromosomal locus of Salmonella typhimurium is essential for the dissimilatory anaerobic reduction of thiosulfate to hydrogen sulfide. The Phs region is a functional operon with three open reading frames, designated PhsA, PhsB, and PhsC, which encode peptides of 82.7, 21.3, and 28.5 kDa, respectively. The products of PhsA and PhsB exhibit significant homology with the catalytic and electron transfer subunits of anaerobic molybdoprotein oxidoreductases. The predicted PhsC product is highly hydrophobic and similar in size to the hydrophobic subunits of the molybdoprotein oxidoreductases containing subunits homologous to PhsA and PhsB. PhsABC appears to encode thiosulfate reductase
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
Results 1 - 4 of 4