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Literature summary for 1.14.14.18 extracted from

  • Cornejo, J.; Beale, S.I.
    Algal heme oxygenase from Cyanidium caldarium. Partial purification and fractionation into three required protein components (1988), J. Biol. Chem., 263, 11915-11921.
    View publication on PubMed

Activating Compound

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

Inhibitors Comment Organism Structure
Sn-protoporphyrin 0.002 mM, 80% inhibition Cyanidium caldarium

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Cyanidium caldarium
-
-

Metals/Ions

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 [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

Organism UniProt Comment Textmining
Cyanidium caldarium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Cyanidium caldarium

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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
-
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