Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Fe/S cluster | heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity | Cyanidium caldarium |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Sn-protoporphyrin | 0.002 mM, 80% inhibition | Cyanidium caldarium |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | - |
Cyanidium caldarium | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity | Cyanidium caldarium |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
heme oxygenase consists of 3 components: a 22000 Da ferredoxin-like Fe/S cluster protein that can be replaced by ferredoxin, a 38000 Da protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a 37000 Da protein with ferredoxin-linked cytochrome c reductase activity | Cyanidium caldarium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyanidium caldarium | - |
- |
- |
Purification (Comment) | Organism |
---|---|
partial | Cyanidium caldarium |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + electron donor + O2 | algal heme oxygenase requires a second reductant in addition to reduced pyridine nucleotide | Cyanidium caldarium | biliverdin + Fe2+ + CO + oxidized eletron donor + H2O | - |
? |