EC Number   |
Metals/Ions |
Reference |
|---|
   1.14.18.3 | Cu2+ |
14.5 atoms per molecule of enzyme pMMO, type II copper centre |
438944 |
| 1.14.18.3 | Iron |
2.5 atoms per enzyme molecule of pMMO |
438944 |
| 1.14.18.3 | Cu2+ |
a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity |
745721 |
| 1.14.18.3 | Cu2+ |
absolutely required, quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase, copper content and binding structure analysis, crystal structures analysis from PDB IDs 3RGB and 3RFR, and modeling, QM-refined structures, detailed overview. Putative mechanism for the reaction of the mononuclear site with methane |
744037 |
| 1.14.18.3 | copper |
an anomalous site modeled as a dinuclear copper cluster. The mononuclear copper site is absent (one His is not conserved), and the zinc replaced by a copper ion |
703343 |
| 1.14.18.3 | Cu2+ |
an integral membrane metalloenzyme, the enzyme has a dicopper active site, structures of the dicopper site of enzyme pMMO, overview. Possible peroxo state of the dicopper site of pMMO from combined quantum mechanics and molecular mechanics calculations. The pMMO active site is considered to contain two Cu ions with a Cu-Cu distance of about 2.58 A within the pmoB subunit. One copper is coordinated by two histidine imidazoles, and another is chelated by a histidine imidazole and primary amine of an N-terminal histidine. The QM region contains the two Cu ions, His33, His137, His139, Tyr374, and Glu35 for the resting state, and, in addition, two oxygen atoms for the peroxo state |
745067 |
| 1.14.18.3 | more |
analysis of the oxidation states and coordination environments of the pMMO metal centers, overview |
674005 |
| 1.14.18.3 | Fe2+ |
As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO |
716109 |
| 1.14.18.3 | Zn2+ |
binds in the copper active site |
745389 |
| 1.14.18.3 | Zn2+ |
can replace Cu2+, enzyme-bound, structure analysis, overview. Zinc binding at the pmoC site in the zinc-soaked structure stabilizes pmoC residues 200-210 |
745305 |
