EC Number   |
Metals/Ions |
Reference |
|---|
   1.16.3.4 | copper |
contains six copper atoms per polypeptide chain and displays optical and electron paramagnetic resonance spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The addition of copper leads to immediate and reversible changes in the optical and electron paramagnetic resonance spectra of the protein, as well as decreased thermal stability of the enzyme and stimulates both the phenoloxidase and ferroxidase activities |
763198 |
| 1.16.3.4 | copper |
four copper atoms per molecule, spectroscopic properties are typical of blue copper oxidase. Presence of copper is essential for CueO-dependent oxidation of 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) and p-phenylenediamine, reactions of EC 1.10.3.2 |
762691 |
| 1.16.3.4 | copper |
in the absence of excess Cu(II), in addition to the normal reduction of the T1 copper, which occurs with a slow rate, a second electron transfer process occurs to an unknown site, possibly the trinuclear cluster, followed by a slow intramolecular electron transfer to T1 copper |
763654 |
| 1.16.3.4 | copper |
mechanism of copper incorporation in CueO is sequential, with type 1 copper being the first to be reconstituted, followed by type 2 and type 3 sites. The copper content of the purified protein is routinely 0.5-0.6 Cu atoms/protein molecule |
763277 |
| 1.16.3.4 | copper |
the affinity of site T4 for Cu(II) shows a KD of 0.0055 microM |
763183 |
| 1.16.3.4 | Cu(I) |
the number of Cu(I) bound is nearly proportional to the methionine-rich loop lengths and to the number of potential Cu(I) ligands in these loops |
762773 |
| 1.16.3.4 | Cu+ |
Cu(I) coordinates to a flexible, methionine-rich sequence |
763245 |
| 1.16.3.4 | Cu+ |
multicopper oxidase |
763026 |
| 1.16.3.4 | Cu2+ |
upon incubation with Cu2+ ions, low active apo-CueOR is converted into the active holo-CueOR in vivo |
728744 |
