The mechanism of haem catabolism. A study of haem breakdown in spleen microsomal fraction and in a model system by 18O labelling and metal substitution.
The mechanism of bile-pigment formation from haem breakdown was studied by using 18O labelling of the molecular oxygen required for macrocyclic ring cleavage. For haem degradation by the spleen microsomal haem oxygenase system, mass spectrometry of the product bilirubin revealed that cleavage occurred by the Two-Molecule Mechanism, i.e. the terminal lactam oxygen atoms in bilirubin were derived from two different oxygen molecules. Similarly, degradation of myoglobin by coupled oxidation with ascorbate and oxygen proceeded via the Two-Molecule Mechanism. Cobalt and manganese complexes of protoporphyrin IX were not degraded by either the haem oxygenase system or the coupled oxidation system. This result suggests that the iron atom possesses unique properties in facilitating porphyrin breakdown.
D000818:Animals; D001663:Bilirubin / Q000378:metabolism; D006418:Heme / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D008861:Microsomes / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism; D011524:Protoporphyrins / Q000378:metabolism; D051381:Rats; D013154:Spleen / Q000378:metabolism / Q000648:ultrastructure
D009211:Myoglobin; D011524:Protoporphyrins; D006418:Heme; D010105:Oxygenases; D001663:Bilirubin