EC Number   |
Metals/Ions |
Reference |
|---|
   7.1.1.4 | copper |
a type B heme-copper oxygen reductase. The binuclear Fea3Cu(B) center is the site of dioxygen chemistry and is involved in the proton translocation mechanism. The catalytic bimetallic Cu(B) center is probed in a number of different states using extended X-ray absorption fine structure (EXAFS) spectroscopy. The oxidized CuB center is four-coordinated with three histidine residues and one oxygen atom. No significant change in the protein structure in the vicinity of Cu(B) is observed upon reduction, apart from the release of the oxo ligand |
720065 |
| 7.1.1.4 | copper |
binds 1 copper B ion per subunit |
719394 |
| 7.1.1.4 | copper |
contains one copper atom |
719514 |
| 7.1.1.4 | copper |
heme-copper enzyme |
724989 |
| 7.1.1.4 | copper |
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 | copper |
the enzyme contains one copper atom |
719793 |
| 7.1.1.4 | copper |
the recombinant subunit SoxH of the SoxM complex contains a correctly inserted binuclear Cu(A) cluster. In recombinant form, the metal interacts with cytochrome c as an artificial electron donor. The physiological electron donor is unknown, since Sulfolobus acidocaldarius does not contain any c-type cytochromes. The purple copper center of SoxM shows a pH dependency with a pKa at 6.4, suggesting protonation of the Cu-ligating histidines. Contains 1.3 Cu atoms per SoxH molecule |
719770 |
| 7.1.1.4 | Cu |
a heme-copper enzyme |
719689 |
| 7.1.1.4 | Cu |
the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu |
719024 |
| 7.1.1.4 | Cu2+ |
contains copper |
741970 |
