The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 188.8.131.52, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 184.108.40.206, dissimilatory sulfite reductase.
with inner- and outer-labeled 35S-thiosulfate, the enzyme reduces only the outer sulfur atom to hydrogen sulfide. No substrates: sulfate, sulfite, tetrathionate, dithionate. No electron donors: reduced nicotinamide adenine dinucleotide, reduced nicotinamide adenine dinucleotide phosphate, reduced glutathione, or cysteine
enzyme catalyzes the stoichiometric production of hydrogen sulfide and sulfite from thiosulfate. The most efficient coupling is obtained with a system containing cytochromes c3. The enzyme exhibits tetrathionate reductase activity. It does not show sulfite reductase activity
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three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3