EC Number   |
Metals/Ions |
Reference |
|---|
    4.2.1.22 | Ca2+ |
contains 0.38 Ca atoms/subunit |
681468 |
| 4.2.1.22 | Co2+ |
97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant |
713958 |
| 4.2.1.22 | Co3+ |
cobalt-substituted variant of hCBS, i.e. Co hCBS, in which CoPPIX replaces FePPIX, i.e. heme. Co(III) hCBS is a unique Co-substituted heme protein: the Co(III) ion is 6-coordinate, low-spin, diamagnetic, and bears a cysteine(thiolate) as one of its axial ligands. Electronic absorption and MCD spectra of the Co-substituted heme protein, overview. Co(III) hCBS is slowly reduced to Co(II) hCBS, which contains a 5-coordinate, low-spin, S = 1/2 Co-porphyrin that does not retain the cysteine(thiolate) ligand. This form of Co(II)hCBS binds NO but not CO. Co(II) hCBS is reoxidized in the air to form a new Co(III) form, which does not contain a cysteine(thiolate) ligand. Maintaining the native heme ligation motif of wild-type Fe hCBS (Cys/His) is essential in maintaining maximal activity in Co hCBS |
715172 |
| 4.2.1.22 | Fe |
contains 0.13 Fe atoms/subunit |
681468 |
| 4.2.1.22 | Fe |
contains 0.67 Fe atoms/subunit, in minimal medium |
681468 |
| 4.2.1.22 | Fe2+ |
contains 0.16 Fe atoms/subunit |
681468 |
| 4.2.1.22 | Fe2+ |
ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process |
678239 |
| 4.2.1.22 | Fe2+ |
heme enzyme, 97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant |
713958 |
| 4.2.1.22 | Fe2+ |
wild-type FePPIX, i.e. heme |
715172 |
| 4.2.1.22 | Fe3+ |
- |
701929 |
