EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.4.52 | Co2+ |
10% of the activity with Mg2+, Mn2+ in presence of Co2+ |
680452 |
| 3.1.4.52 | Fe2+ |
trinuclear Fe binding site located at the bottom of the HD-GYP domain cavity formed by the two claws of the open chela. Residues E185, H189, H221, D222, H250, H276, H277, and D305 are involved in metal binding |
730416 |
| 3.1.4.52 | Iron |
accommodates di- and triiron active site |
749912 |
| 3.1.4.52 | Iron |
heme protein with remarkable stability against electron transfer to O2. Oxy-enzyme is only 30% oxidized to the ferric form after 8 h in airsaturated Tris buffer pH 8.0, 23°C |
678127 |
| 3.1.4.52 | Mg2+ |
activates |
730749 |
| 3.1.4.52 | Mg2+ |
Mn2+ ion can replace Mg2+ ion in catalysis |
692857 |
| 3.1.4.52 | Mg2+ |
or Mn2+, absolutely required, with Mn2+ being slightly more efficient |
680452 |
| 3.1.4.52 | Mg2+ |
or Mn2+, required, with Mg2+ being more efficient. Enzyme activity increases with with increasing Mg2+ concentration up to 25 mM MgCl2 |
680631 |
| 3.1.4.52 | Mg2+ |
required |
680630, 713841, 715164 |
| 3.1.4.52 | Mg2+ |
required for catalysis |
730416 |
