EC Number   |
Metals/Ions |
Reference |
|---|
    7.1.1.9 | Ca2+ |
contains one Ca2+ per enzyme, tighly bound Ca2+ plays a structural role in the enzyme. Mutant enzyme D485A is active, binds to Ca2+ reversibly, and exhibits the red shift in the heme a absorption spectrum upon Ca2+ binding for both reduced and oxidized states of heme a. Sodium ions reverse the Ca2+-induced red shift of heme a and dramatically decrease the rate of Ca2+ binding to the mutant enzyme. With the mutant enzyme, 1 Ca2+ competes with 1 Na+ for the binding site |
657937 |
| 7.1.1.9 | copper |
- |
696427, 698934, 699664 |
| 7.1.1.9 | copper |
contains copper |
724497, 725643 |
| 7.1.1.9 | copper |
Cox17p specifically binds Cu(I) at a molar copper content of 3.3 under redzuced conditions and significantly activates the mitochondrial. The Cu-Cox17p complex is maintained between pH values from 5.0 to 7.7. Cu is completely released from Cox17p at pH 8.0. The stringent selectivity of Cox17p for cipper is required for enzyme activation |
657776 |
| 7.1.1.9 | copper |
oxidation of copper in cytochrome c oxidase of Prnp-/- mice is similar to that in Prnp+/+ mice |
694987 |
| 7.1.1.9 | Cu |
- |
395991, 395992, 395996, 395999, 396000, 396001, 396002, 396003, 396006, 396008, 396012, 396026, 396029, 396035, 396036, 396038, 396049, 396050, 396069, 396071, 396073, 396074, 396075, 396077, 396081, 396083, 396085, 396088, 396092, 396109, 691038, 692575, 698272, 698494, 700992 |
| 7.1.1.9 | Cu |
0.7 copper atoms in minimal structure unit composed of the three subunits |
396115 |
| 7.1.1.9 | Cu |
0.96 mol Cu per mol of enzyme |
396136 |
| 7.1.1.9 | Cu |
2 copper ions at the CuA site |
396122 |
| 7.1.1.9 | Cu |
2 Cu atoms per enzyme molecule |
396024 |
