EC Number   |
Cofactor |
Reference |
|---|
    7.1.1.3 | heme |
the enzyme contains a low-spin b-like heme and a high-spin 6-like heme, designated cytochromes b and o respectively |
714885 |
| 7.1.1.3 | heme |
the enzyme contains the low spin hexacoordinate heme b558 and the high spin pentacoordinate hemes b595 and d |
741957 |
| 7.1.1.3 | heme |
the enzyme contains two b- and one d-type hemes as cofactors |
742510 |
| 7.1.1.3 | heme |
the enzyme possesses two hemes (18.1 ng/mg) |
714129 |
| 7.1.1.3 | heme |
the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water |
714132 |
| 7.1.1.3 | heme |
the purified oxidase contains both protoheme and heme O |
714285 |
| 7.1.1.3 | heme |
the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family |
714135 |
| 7.1.1.3 | ubiquinol-8 |
- |
714997, 715000 |
| 7.1.1.3 | ubiquinone-8 |
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions |
715003 |
| 7.1.1.3 | ubiquinone-8 |
the enzyme contains one equivalent of ubiquinone-8 |
714308 |
