| Dimethylsulfoxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.5.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
DMSO reductase is a molybdenum-containing enzyme that catalyzes reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). This enzyme serves as the terminal reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then reduced to water.
DMSO reductase (DMSOR) and other members of the DMSO reductase family are unique to bacteria and archaea. Enzymes of this family in anaerobic oxidative phosphorylation and inorganic-donor-based lithotrophic respiration. These enzymes have been engineered to degrade oxoanions.[1][2][3] DMSOR catalyzes the transfer of two electrons and one oxygen atom in the reaction: The active site of DMSOR contains molybdenum, which is otherwise rare in biology.[2]
- ^ Kappler U, Schäfer H (2014). "Chapter 11. Transformations of Dimethylsulfide". In Kroneck PM, Torres ME (eds.). The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 279–313. doi:10.1007/978-94-017-9269-1_11. ISBN 978-94-017-9268-4. PMID 25416398.
- ^ a b McEwan AG, Kappler U (2004). "The DMSO Reductase Family of Microbial Molybdenum Enzymes" (PDF). Australian Biochemist. 35 (3): 17–20. Archived from the original (PDF) on 2014-03-07. Retrieved 2014-02-27.
- ^ McEwan AG, Ridge JP, McDevitt CA, Hugenholtz P (2002). "The DMSO Reductase Family of Microbial Molybdenum Enzymes; Molecular Properties and Role in the Dissimilatory Reduction of Toxic Elements". Geomicrobiology Journal. 19 (1): 3–21. Bibcode:2002GmbJ...19....3M. doi:10.1080/014904502317246138. S2CID 85091949.