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Literature summary for 1.8.5.3 extracted from
- Addressing serine lability in a paramagnetic dimethyl sulfoxie reductase catalytic intermediate (2021), Inorg. Chem., 60, 9233-9237 .
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cereibacter sphaeroides | Q57366 | Rhodobacter sphaeroides | - |
| Rhodobacter capsulatus | Q52675 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylsulfoxide + menaquinol | - |
Rhodobacter capsulatus | dimethylsulfide + menaquinone + H2O | - |
? | |
| dimethylsulfoxide + menaquinol | - |
Cereibacter sphaeroides | dimethylsulfide + menaquinone + H2O | - |
? | |
Synonyms
| 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
| 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
| 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 |
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