Claim: Thiosulfate dehydrogenase (an oxidoreductase which is an enzyme that catalyzes the transfer of electrons from one molecule) the N-terminal domain is structurally homologous, and some domain contains a covalently bound iron-containing heme molecule.
Evidence: Thiosulfate dehydrogenase (abbreviated as TsdA) (EC ) is an enzyme that catalyzes the chemical reaction: This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. 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. The single active site of the enzyme is located in between the two domains (closer to the C-terminus domain) near the central iron heme.