EC Number   |
Metals/Ions |
Reference |
|---|
    1.17.4.1 | Ca2+ |
activity depends on Ca2+ |
437979 |
| 1.17.4.1 | Co2+ |
class II enzymes contain cobalamin as cofactor |
715085 |
| 1.17.4.1 | Fe |
class I enzymes contain diferric(III)-tyrosyl radical cofactor |
715085 |
| 1.17.4.1 | Fe2+ |
- |
687333 |
| 1.17.4.1 | Fe2+ |
assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview |
702226 |
| 1.17.4.1 | Fe2+ |
class Ia ribonucleotide reductase subunit R2 contains a diiron active site, active-site crystal structures of the Fe(II)Fe(II) and Fe(III)Fe(III) clusters, overview |
715170 |
| 1.17.4.1 | Fe2+ |
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2 |
716920 |
| 1.17.4.1 | Fe2+ |
classIb RNR biferrous site structure, the spectroscopically defined active site contains a 4-coordinate and a 5-coordinate Fe(II), weakly antiferromagnetically coupled via mu-1,3-carboxylate bridges, detailed spectral analysis, overview |
702216 |
| 1.17.4.1 | Fe2+ |
each beta-protomer of the small betabeta subunit (R2) contains a binuclear iron cluster with inequivalent binding sites: FeA and FeB. The majority of the protein binds only one Fe(II)atom per betabeta subunit. Additional iron occupation can be achieved upon exposure to O2 or in high glycerol buffers. The binding of the first Fe(II) atom to the active site in a beta-protomer (beta1) induces a global protein conformational change that inhibits access of metal to the active site in the other beta-protomer (betaII). The binding of the same Fe(II) atom also induces a local effect at the active site in beta1-protomer, which lowers the affinity for metal in the A-site |
659447 |
| 1.17.4.1 | Fe2+ |
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. The R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview. Structure modelling |
704612 |
