EC Number |
Metals/Ions |
Reference |
---|
1.8.99.5 | Cu |
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory hemecopper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2 |
743347 |
1.8.99.5 | Fe |
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A |
743347 |
1.8.99.5 | Iron |
20 mol of iron per mol of enzyme |
733765 |
1.8.99.5 | Iron |
20 to 21 nonheme iron atoms per enzyme molecule |
394043 |
1.8.99.5 | Iron |
24 mol of iron per mol of enzyme |
394066 |
1.8.99.5 | Iron |
contains 22 non-heme iron atoms per molecule |
734637 |