EC Number   |
Cofactor |
Reference |
|---|
   7.1.1.4 | cytochrome |
the active respiratory terminal oxidase segment of Sulfolobus sp. strain 7 contains one non-CO-reactive b-type cytochrome (b562) and two different a-type cytochromes (a583 and aa3), in addition to one copper and a Rieske-type FeS cluster, which, as a whole, function as an active caldariellaquinol oxidase supercomplex |
722598 |
| 7.1.1.4 | heme |
- |
741970 |
| 7.1.1.4 | heme |
a heme-copper enzyme |
719689 |
| 7.1.1.4 | heme |
a three-redox-centers enzyme. The enzyme has two heme with apparent redox potentials 215 mV and 415 mV at pH 5.4, and a heme a3-CuB center |
719396 |
| 7.1.1.4 | heme |
a type B heme-copper oxygen reductase |
720065 |
| 7.1.1.4 | heme |
binds 2 heme groups per subunit |
719394 |
| 7.1.1.4 | heme |
heme-copper enzyme |
724989 |
| 7.1.1.4 | heme |
hemeprotein. The single subunit (38000-40000 Da) contains two heme a molecules. The redox potentials of the heme centres are +220 mV and +370 mV, respectively. One heme is a heme-a3 centre |
396010 |
| 7.1.1.4 | heme |
hemoprotein, contains two heme A molecules, one heme is a heme a3-centre, presence of a low-spin and a high-spin heme species |
719514 |
| 7.1.1.4 | heme |
the complex contains four haems A. Two haems belong to the 'cytochrome oxidase' part of the complex and two are probably bound to be apocytochrome b (SoxC) and responsible for the 586 nm absorption peak |
719354 |
