摘要
利用微量热法和热动力学方程研究了过氢化氢酶反应。该反应遵循Michaelis-Menten动力学,298.15K和pH7.0时,其米氏常数、酶转换数以及摩尔反应焓分别为2.36×10-2mol/L、1.20×104s-1和-83.67kJ·mol-1。过氧化氢酶反应后期对底物是一级反应,其总反应速度常数和一级速度常数分别为ko=6.31×105L·mol-1·s-1和k1=6.31×105/[Eo]s-1。该反应服从Ogura机理,其酶-底物三元复合物的分解速度常数为6.00×103s-1。
Microcalorimetry and thermokinetic equations were used to study H2O2 decomposition by beef liver catalase.The catalase reaction obeyed the Michaelis-Menten kinetics,and at 298.15 K and pH 7.0,the Michaelis constant (Km),the turnover number and the molar enthalpy(ΔrHm)of the reaction were 2.36×10-2 mol/L,1.20×104s-1 and-83.67 kJ·mol-1,respectively.The later period of catalase reaction was a first order reaction for H2O2,=6.31×105L·mol-1·s-1 and k1=6.31×10-5/[Eo]s-1,respectively.The catalase reaction obeyed Ogura mechanism,and the ternary complex decomposition rate constant was 6.00×103s-1.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
1995年第6期924-928,共5页
Chemical Journal of Chinese Universities
基金
国家自然科学基金
关键词
微量热法
过氧化氢酶
米氏常数
反应机理
Microcalorimetry Catalase Michaelis constant Thermokinetic equation Reaction mechanism