EC Number   |
Metals/Ions |
Reference |
|---|
   1.10.3.3 | copper |
electronic structure of blue copper sites |
439914 |
| 1.10.3.3 | copper |
enzyme contains a set of 1 type I, 1 type II and a pair of type III copper ions at its active site |
439917 |
| 1.10.3.3 | copper |
enzyme contains type I, type II and type III copper atoms in the ratio 1/2/2, 4 copper atoms/enzyme |
439929 |
| 1.10.3.3 | copper |
evidence that the coordination environment and electronic structure of the type 1 copper is similar to those of plastocyanin and azurin |
439914 |
| 1.10.3.3 | copper |
measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme |
439900 |
| 1.10.3.3 | copper |
multi-copper oxidase |
764908 |
| 1.10.3.3 | copper |
native enzyme contains two type 1, two type 2 and four type 3 copper ions |
439904 |
| 1.10.3.3 | copper |
principal active site comprised of one type I, one type II and a pair of type III coppers |
439917 |
| 1.10.3.3 | copper |
the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate |
684895 |
| 1.10.3.3 | copper |
type 2 copper may be part of the ascorbate binding site |
439915 |
