Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. III. Properties of thiosulfate-oxidizing enzyme and proposed pathway of thiosulfate oxidation

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Abstract
Thiosulfate-oxidizing enzyme was purified from Thiobacillus thioparus extracts 120- to 160-fold and the properties were studied. The enzyme had a molecular weight of 115 000 and contained 2 moles of non-heme iron. Ferricyanide was a much better electron acceptor than cytochrome c, but with cytochrome c the Km for thiosulfate was lowered from 0.1 mM to 5 μM and the pH response of the enzyme changed. Sulfite was a very strong inhibitor destroying 50% of the activity at 5 μM. The inhibition was time-dependent and essentially irreversible. Properties of the T. thioparus enzyme were compared to those of thiosulfate-oxidizing enzyme isolated from Thiobacillus neapolitanus and Ferrobacillus ferrooxidans. A pathway of thiosulfate oxidation is proposed, and metabolic roles of various enzymes studied in T. thioparus are discussed.
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