[辣根过氧化物酶存在下过氧化氢氧化邻联茴香胺的动力学研究]
[Kinetic study of o-dianisidine oxidation by hydrogen peroxide in the presence of horseradish peroxidase].
作者信息
Lebedeva O V, Ugarova N N, Berezin I V
出版信息
Biokhimiia. 1977 Aug;42(8):1372-9.
A kinetic study of o-dianisidine oxidation by hydrogen peroxide in the presence of horseradish peroxidase within the pH range of 3.7-9.0 has been carried out. It was shown that the reaction of o-dianisidine peroxidase oxidation obeys the Michaelis--Menten kinetics; the kcat and Km values within the pH range used were determined. The optimum of peroxidase catalytic activity during o-dianisidine oxidation was observed at pH 5.0-6.0. The kinetic pattern of the reaction is discussed. It was demonstrated that deprotonation of the group at pK 6.5 decreases the kcat value 60 times. At pH greater than 8.0 an additional ionogenic group controls the enzyme activity.
在pH值3.7 - 9.0范围内，对辣根过氧化物酶存在下过氧化氢氧化邻联茴香胺的动力学进行了研究。结果表明，邻联茴香胺过氧化物酶氧化反应遵循米氏动力学；测定了所用pH范围内的kcat和Km值。在邻联茴香胺氧化过程中，过氧化物酶催化活性的最佳值出现在pH 5.0 - 6.0。讨论了该反应的动力学模式。结果表明，pK 6.5处基团的去质子化使kcat值降低60倍。在pH大于8.0时，另一个离子ogenic基团控制酶的活性。
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