EC Number   |
Metals/Ions |
Reference |
|---|
    1.15.1.2 | Ca2+ |
at the dimer interface coordinated by eight oxygen atoms, Ser87, Thr89 from both monomers, and two water molecules |
686522 |
| 1.15.1.2 | Fe |
2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction |
715670 |
| 1.15.1.2 | Fe |
the enzyme contains a catalytic nonheme iron centre coordinated by four histidine ligands and one cysteine ligand |
713642 |
| 1.15.1.2 | Fe2+ |
1Fe SOR is a non-heme iron enzyme, iron binding and reaction mechanism, detailed overview |
687278 |
| 1.15.1.2 | Fe2+ |
1Fe-SOR or neelaredoxin class of superoxide reductases |
687820 |
| 1.15.1.2 | Fe2+ |
a 1Fe-SOR, the iron centre is highly sensitive to photoreduction. The N-terminal loop of the protein, containing the characteristic EKHxP motif, reveals an unusually high flexibility regardless of the iron redox state. Each GiSOR monomer displays a solvent-exposed active site containing one Fe atom. The high solvent accessibility of the metal has been proposed to be important for the catalytic function of the enzyme, as it ensures easy access of superoxide anion to the active site and its prompt reduction to hydrogen peroxide. The Fe atom displays octahedral coordination geometry and is coordinated by residues located in loops connecting beta-strands: the imidazole rings of His19, His40, His46 and His102 in the equatorial plane, with the Cys99 S atom and one carboxylate O atom from Glu17 occupying the two axial positions |
743942 |
| 1.15.1.2 | Fe2+ |
a non-heme iron enzyme, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112, metal binding site structure, overview |
746425 |
| 1.15.1.2 | Fe2+ |
a non-heme iron enzyme, isolation of coordinatively unsaturated, mononuclear five coordinate thiolate iron complexes, including [FeIII-(S2Me2N3(Pr,Pr))]+, [FeIII(S2Me2N3-(Et,Pr))]+, and [FeII(SMe2N4(tren))]+ |
684111 |
| 1.15.1.2 | Fe2+ |
a non-heme, iron-containing enzyme, in the catalytically active reduced state, SORs contain a high-spin FeII center ligated by four equatorial histidine units and one apical cysteinate residue trans to an open site. Additionally, a number of SORs also contain a second rubredoxin-like [Fe(SCys)4] center, complex formation, kinetics, and electrochemistry, overview |
686523 |
| 1.15.1.2 | Fe2+ |
a nonheme iron-containing enzyme, 2Fe-SOR or desulfoferrodoxin class of superoxide reductases |
674937 |
