血红素分解代谢的机制。通过18O标记和金属替代对脾脏微粒体部分和模型系统中血红素分解的研究。
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.
作者信息
King R F, Brown S B
出版信息
Biochem J. 1978 Jul 15;174(1):103-9. doi: 10.1042/bj1740103.
Abstract
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.
摘要
通过对大环环裂解所需分子氧进行(^{18}O)标记，研究了血红素分解形成胆色素的机制。对于脾脏微粒体血红素加氧酶系统对血红素的降解，产物胆红素的质谱分析表明，裂解是通过双分子机制发生的，即胆红素中的末端内酰胺氧原子来自两个不同的氧分子。同样，通过抗坏血酸和氧的偶联氧化对肌红蛋白的降解也通过双分子机制进行。原卟啉IX的钴和锰配合物既不被血红素加氧酶系统降解，也不被偶联氧化系统降解。这一结果表明，铁原子在促进卟啉分解方面具有独特的性质。
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本文引用的文献
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HAEM catabolism and coupled oxidation of haemproteins.血红素分解代谢与血红素蛋白的偶联氧化
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Proc Natl Acad Sci U S A. 1968 Oct;61(2):748-55. doi: 10.1073/pnas.61.2.748.
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