Thiosulfate dehydrogenase

Thiosulfate dehydrogenase (abbreviated as TsdA) (EC 1.8.2.2) is an enzyme that catalyzes the chemical reaction: Thiosulfate dehydrogenase (abbreviated as TsdA) (EC 1.8.2.2) is an enzyme that catalyzes the chemical reaction: Thus, the two substrates of this enzyme are thiosulfate and ferricytochrome c, whereas its two products are tetrathionate and ferrocytochrome c. Thiosulfate dehydrogenase homologues have been isolated from numerous bacterial species and differ slightly in structure but have analogous function and mechanism of sulfur oxidation. The enzyme is similar in both function and structure to a few enzymes in the Sox sulfur oxidation pathway. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is thiosulfate:ferricytochrome-c oxidoreductase. Other names in common use include tetrathionate synthase, thiosulfate oxidase, thiosulfate-oxidizing enzyme, and thiosulfate-acceptor oxidoreductase. Thiosulfate dehydrogenase, isolated from the appreciably studied bacterial strain Allochromatium vinosum (253 peptide chain length, 25.8 kDa) is composed of two catalytic domains, each similar to cytochrome c, linked by a long unstructured peptide chain. The N-terminal domain is structurally homologous to the SoxA family of cytochrome enzymes while the C-terminal domain is representative of the standard mitochondrial cytochrome c family fold with high similarity to nitrite reductase from P. haloplanktis. Each domain contains a covalently bound iron-containing heme molecule separated by a short distance of 8.1 Å which assists with rapid electron transfer. Both the N and C terminus domains contain 4 α helices (surrounding the heme in the corresponding domain) and a two-stranded anti-parallel β sheet, suggesting the enzyme resulted from a gene duplication event.