过氧化氢酶与过氧乙酸反应生成化合物I。
Formation of compound I by the reaction of catalase with peroxoacetic acid.
作者信息
Jones P, Middlemiss D N
出版信息
Biochem J. 1972 Nov;130(2):411-5. doi: 10.1042/bj1300411.
Abstract
- The formation of Compound I by the reactions of bacterial and ox liver catalases with peroxoacetic acid was examined. In both cases the process occurs almost entirely by reaction of catalase with un-ionized peroxoacetic acid molecules. The result suggests an important role for the bound peroxidic proton in the enzyme-substrate interaction. 2. The peroxidatic properties of the Compounds I formed when peroxoacetic acid was used were examined by studying the oxidations of ethanol and formate; the results closely resemble those previously reported when H(2)O(2) and alkyl hydroperoxides were used. 3. Compound I formed with bacterial catalase and peroxoacetic acid is remarkably stable in the absence of added donor and the preparation has considerable potential for detailed studies of the nature of this intermediate.
摘要
- 研究了细菌过氧化氢酶和牛肝过氧化氢酶与过氧乙酸反应生成化合物I的过程。在这两种情况下，该过程几乎完全是由过氧化氢酶与未电离的过氧乙酸分子反应引起的。该结果表明结合的过氧质子在酶-底物相互作用中起重要作用。2. 通过研究乙醇和甲酸盐的氧化反应，考察了用过氧乙酸生成的化合物I的过氧化物性质；结果与先前报道的使用H₂O₂和烷基氢过氧化物时的结果非常相似。3. 由细菌过氧化氢酶和过氧乙酸形成的化合物I在没有添加供体的情况下非常稳定，该制剂对于详细研究这种中间体的性质具有很大的潜力。
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本文引用的文献
1
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2
The enzymesubstrate compounds of bacterial catalase and peroxides.细菌过氧化氢酶和过氧化物的酶底物化合物。
Biochem J. 1950 Apr;46(4):402-14. doi: 10.1042/bj0460402.
3
The catalase-hydrogen peroxide system. A theoretical appraisal of the mechanism of catalase action.过氧化氢酶-过氧化氢系统。对过氧化氢酶作用机制的理论评估。
Biochem J. 1968 Dec;110(4):621-9. doi: 10.1042/bj1100621.
4
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