Acta Chimica Sinica ›› 1989, Vol. 47 ›› Issue (1): 49-56. Previous Articles     Next Articles

Original Articles

细胞色素P-450酶模型的研究:过氧化物的化学反应机理

徐丰;TRAYLOR, T.G.   

  1. 美国加利福尼亚大学化学系
  • 出版日期:1989-01-15 发布日期:1989-01-15

Cytochrome P-450 model: Mechanistic study of peroxides chemistry

XU FENG;TRAYLOR, T.G.   

  • Online:1989-01-15 Published:1989-01-15

The cytochrome P 450 and other peroxidases which contain an Fe-porphyrin active center play a key role in H2O2 removal from biol. systems. The mechanistic studies on this reaction catalyzed by model iron porphyrins have been discussed. In the active intermediate (Fe-oxene porphyrin) forming step, a general base catalyzed heterolytic-type cleavage of O-O bond scheme is consistent with most experiment results from direct observations of reactions in solution and the comparisons with thermolysis studies of peroxides, which is a well known homolytic. A direct, rapid reaction of peroxides with the Fe-oxene intermediate can take place. Peroxides react as substrates as well as oxidants. Those systems could provide convenient models to study the enzyme catalysis.

Key words: ENZYME, OXIDATION, REACTION MECHANISM, IRON COMPLEX, CYTOCHROME, PEROXIDE, FRACTURE MECHANISM, ACTIVE SITE, PORPHINE

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