EC Number   |
Inhibitors  |
Structure |
|---|
   1.14.18.3 | 2-Heptyl-4-hydroxyquinoline-N-oxide |
pMMO, at 0.05 mM |
   |
| 1.14.18.3 | Acetylene |
pMMO |
|
| 1.14.18.3 | Acetylene |
complete inhibition at 0.1 mM |
|
| 1.14.18.3 | Acetylene |
is a competitive inhibitor of pMH, interacts with its substrate-binding center |
|
| 1.14.18.3 | Acetylene |
4.3% residual activity at 10% (v/v) |
|
| 1.14.18.3 | Acetylene |
a suicide inhibitor of pMMO, inactivation of the particulate methane monooxygenase (pMMO): the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived fromin-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO are controlled tightly within the transmembrane domain |
|
| 1.14.18.3 | copper |
copper contents per 100 kDa alphabetagamma protomer of 15-20, eight to ten, two to three and two. Mixture of Cu(I) and Cu(II), copper cluster with a short Cu-Cu distance of 2.51 A that increases to 2.65 A upon chemical reduction with dithionite. The pMMO contains a mononuclear type 2Cu(II) centre and some type of copper cluster |
|
| 1.14.18.3 | copper |
contains approximately two copper ions per 100 kDa protomer, type 2 Cu(II) present as two distinct species, mixture of Cu(I) and Cu(II). Short Cu-Cu interaction at 2.51 A. Di-copper centre plays an important functional role in pMMO, whereas the mononuclear copper centre is not critical |
|
| 1.14.18.3 | copper |
two-coordinate (His2) mononuclear copper site and an anomalous site modeled as a dinuclear copper cluster. The cluster has one Cu ion bound by two His imidazoles and another by an imidazole and amino group of the pmoB N-terminal His |
|
| 1.14.18.3 | Cu+ |
pMMO |
|
