EC Number |
Metals/Ions |
Reference |
---|
1.14.18.3 | copper |
the enzyme contains about 2.3 copper ions per 100 kDa protomer the enzyme contains a mixture of Cu+ and Cu2+ |
726954 |
1.14.18.3 | copper |
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron |
745389 |
1.14.18.3 | copper |
the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase |
746420 |
1.14.18.3 | copper |
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme. The copper ion interacts with three or four nitrogenic ligands, EPR-active copper |
657810 |
1.14.18.3 | Cu+ |
pMMO, requirement for, contains 12-15 Cu+ ions per molecule of enzyme |
438952 |
1.14.18.3 | Cu+ |
the C-terminal domain of PmoB in pMMO is a reservoir for Cu(I) with properties similar to those of the E-cluster copper ions in the intact holoenzyme |
685113 |
1.14.18.3 | Cu2+ |
14.5 atoms per molecule of enzyme pMMO, type II copper centre |
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 | 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 |