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化学学报
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化学学报 ›› 1989, Vol. 47 ›› Issue (1): 49-56. 上一篇    下一篇

研究论文

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
  • 发布日期:1989-01-15

Cytochrome P-450 model: Mechanistic study of peroxides chemistry

XU FENG;TRAYLOR, T.G.   

  • Published:1989-01-15

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含有铁卟啉化合物活性中心的细胞色素P-450和其它过氧化物酶具有重要的生物化学功能. 本文讨论了铁卟啉模型物模拟这些酶功能的反应机理. 通过与已知的过氧化物中氧氧键均裂机理的比较, 以及对大部分溶液反应的研究, 表明在过氧化物(包括过氧酸)与铁卟啉生成活性中间体( Fe=O^+.)的过程中, 氧氧键的异裂机理占主导地位. 过氧化物如同其它氧化剂受物(如烯烃)一样, 能快速地直接与 FeO^+反应. 以铁卟啉为催化剂的过氧化物反应体系为我们提供了研究模拟催化酶的人工模型体系.

关键词: 酶, 氧化, 反应机理, 铁络合物, 细胞色素, 过氧化物, 断裂机理, 活性部位, 卟吩

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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