EC 1.8.2.2 - Thiosulfate dehydrogenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.8.2.2

Names

Accepted name:
thiosulfate dehydrogenase
Other names:
tetrathionate synthase
thiosulfate oxidase
thiosulfate-acceptor oxidoreductase
thiosulfate-oxidizing enzyme
tsdA (gene name)
Systematic name:
thiosulfate:ferricytochrome-c oxidoreductase

Reaction

Comments:

The enzyme catalyses the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons. In many bacterial species the enzyme is a diheme c-type cytochrome. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, a second diheme cytochrome (TsdB) acts as the electron acceptor. However, some organisms, such as Allochromatium vinosum, lack TsdB. The electron acceptor in these organisms may be the high-potential iron-sulfur protein (HiPIP).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050338
CAS Registry Number: 9076-88-4
UniProtKB/Swiss-Prot:

References

  1. Lu, W.-P. and Kelly, D.P.
    Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and 'trithionate hydrolase' from Thiobacillus tepidarius.
    J. Gen. Microbiol. 134: 877-885 (1988).
  2. Fukumori, Y. and Yamanaka, T.
    A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum.
    Curr. Microbiol. 3: 117-120 (1979).
  3. Liu, Y. W., Denkmann, K., Kosciow, K., Dahl, C., Kelly, D. J.
    Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria.
    Mol. Microbiol. 88: 173-188 (2013). [PMID: 23421726]
  4. Brito, J. A., Denkmann, K., Pereira, I. A., Archer, M., Dahl, C.
    Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum: structural and functional insights into thiosulfate oxidation.
    J. Biol. Chem. 290: 9222-9238 (2015). [PMID: 25673691]
  5. Kurth, J. M., Brito, J. A., Reuter, J., Flegler, A., Koch, T., Franke, T., Klein, E. M., Rowe, S. F., Butt, J. N., Denkmann, K., Pereira, I. A., Archer, M., Dahl, C.
    Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase.
    J. Biol. Chem. 291: 24804-24818 (2016). [PMID: 27694441]

[EC 1.8.2.2 created 1990]