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Literature summary for 1.14.13.25 extracted from
- Structural model studies for the high-valent intermediate Q of methane monooxygenase from broken-symmetry density functional calculations (2008), Inorg. Chim. Acta, 361, 973-986.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | contains one axial water which also H-bonds to both side chains of Glu243 and Glu114, and one bidentate carboxylate group from the side chain of Glu144, which is likely to represent the active site of MMOH-Q | synthetic construct |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | contains an Fe4+(micro-O)2Fe4+ center. A terminal hydroxo and a protonated His147 which is dissociated from a nearby Fe, is more asymmetric in its Fe(micro-O)2Fe diamond core, and is another very good candidate for intermediate Q | synthetic construct |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| synthetic construct | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MMO | - |
synthetic construct |
| MMOH | - |
synthetic construct |
| soluble methane monooxygenase | - |
synthetic construct |
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