KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of iron mineralization and of Fe(II) oxidation and thermodynamics, overview | Pyrococcus furiosus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | also other oxoanions, besides phosphate and vanadate, increase the oxidation rate of iron | Pyrococcus furiosus | |
phosphate | phosphate does not affect the oxidation rate of the first 48 Fe(II) per ferritin aerobically added to apoferritin. But, it does increase the iron-oxidation rate of subsequent additions of 48 Fe(II) per ferritin by a factor of 6. Phosphate increases the oxidation rate of iron | Pyrococcus furiosus | |
vanadate | increases the oxidation rate of iron | Pyrococcus furiosus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 Fe2+ + 4 H+ + O2 | Pyrococcus furiosus | - |
4 Fe3+ + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 Fe2+ + 4 H+ + O2 | - |
Pyrococcus furiosus | 4 Fe3+ + 2 H2O | - |
? | |
additional information | competitive binding with Zn2+ | Pyrococcus furiosus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | 25 | assay at | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Pyrococcus furiosus |
General Information | Comment | Organism |
---|---|---|
additional information | structure of the diiron binding site of ferritin, overview | Pyrococcus furiosus |
physiological function | ferritin is a ubiquitous iron-storage protein that has 24 subunits. Each subunit of ferritins that exhibit high Fe2+ oxidation rates has a diiron binding site, the socalled ferroxidase center. The role of the ferroxidase center appears to be essential for the iron-oxidation catalysis of ferritins | Pyrococcus furiosus |