EC Number   |
Metals/Ions |
Reference |
|---|
    1.11.1.21 | CO |
complexed with the enzyme, structure determination, binding kinetics |
654769 |
| 1.11.1.21 | Fe |
dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant |
674523 |
| 1.11.1.21 | Fe2+ |
1 mM, 110% of initial activity |
743032 |
| 1.11.1.21 | Fe2+ |
dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant |
674523 |
| 1.11.1.21 | Fe2+ |
enzyme contains a heme modified with a special hydroperoxide group added to ring I |
656158 |
| 1.11.1.21 | Fe2+ |
enzyme contains heme |
654755 |
| 1.11.1.21 | Fe2+ |
heme |
654706 |
| 1.11.1.21 | Fe2+ |
in the heme group |
764015, 764804, 764806, 765180, 765867 |
| 1.11.1.21 | Fe2+ |
iron is present at 1 atom per homodimer |
701415 |
| 1.11.1.21 | Fe2+ |
the bacterial manganese-dependent SOD A when bound to iron has peroxidase activity |
741973 |
