Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylsulfoxide + menaquinol | Rhodobacter capsulatus | - |
dimethylsulfide + menaquinone + H2O | - |
? | |
dimethylsulfoxide + menaquinol | Cereibacter sphaeroides | - |
dimethylsulfide + menaquinone + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | Q57366 | Rhodobacter sphaeroides | - |
Rhodobacter capsulatus | Q52675 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylsulfoxide + menaquinol | - |
Rhodobacter capsulatus | dimethylsulfide + menaquinone + H2O | - |
? | |
dimethylsulfoxide + menaquinol | - |
Cereibacter sphaeroides | dimethylsulfide + menaquinone + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
dimethyl sulfoxid reductase | - |
Rhodobacter capsulatus |
dimethyl sulfoxie reductase | - |
Cereibacter sphaeroides |
DmsA | - |
Cereibacter sphaeroides |
DMSOR | - |
Rhodobacter capsulatus |
DMSOR | - |
Cereibacter sphaeroides |
dorA | - |
Rhodobacter capsulatus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
molybdenum cofactor | two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview | Rhodobacter capsulatus | |
molybdenum cofactor | two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview | Cereibacter sphaeroides |
General Information | Comment | Organism |
---|---|---|
evolution | dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter capsulatus DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle | Rhodobacter capsulatus |
evolution | dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter sphaeroides DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle | Cereibacter sphaeroides |
additional information | two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview | Rhodobacter capsulatus |
additional information | two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview | Cereibacter sphaeroides |