| EC |
1.8.2.6 |
| Accepted name: |
S-disulfanyl-L-cysteine oxidoreductase |
| Reaction: |
[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+ |
| Other name(s): |
SoxCD; sulfur dehydrogenase |
| Systematic name: |
[SoxY protein]-S-disulfanyl-L-cysteine:cytochrome-c oxidoreductase |
| Comments: |
The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Friedrich, C.G., Rother, D., Bardischewsky, F., Quentmeier, A. and Fischer, J. Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism. Appl. Environ. Microbiol. 67 (2001) 2873–2882. [DOI] [PMID: 11425697] |
| 2. |
Bardischewsky, F., Quentmeier, A., Rother, D., Hellwig, P., Kostka, S. and Friedrich, C.G. Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity. Biochemistry 44 (2005) 7024–7034. [DOI] [PMID: 15865447] |
| 3. |
Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12:e0173395 (2017). [DOI] [PMID: 28257465] |
|
| [EC 1.8.2.6 created 2018] |
| |
|
| |
|
Printable version