Ralston I M, Dunford H B, Wauters J, Heremans K
Biophys J. 1981 Oct;36(1):311-4. doi: 10.1016/S0006-3495(81)84731-5.
Reactions of ferric horseradish peroxidase with hydrogen cyanide and hydrogen peroxide were studied as a function of pressure. Activation volumes are small and differ in sign (delta V = 1.7 +/- 0.5 ml/mol for peroxidase + HCN and -1.5 +/- 0.5 ml/mol for peroxidase + H2O2). The temperature dependence of cyanide binding to horseradish peroxidase was also determined. A comparison is made of relevant parameters for cyanide binding and compound I formation.
研究了辣根过氧化物酶与氰化氢和过氧化氢的反应随压力的变化情况。活化体积较小且符号不同(过氧化物酶 + 氰化氢时ΔV = 1.7 ± 0.5 ml/mol,过氧化物酶 + 过氧化氢时为 -1.5 ± 0.5 ml/mol)。还测定了氰化物与辣根过氧化物酶结合的温度依赖性。对氰化物结合和化合物I形成的相关参数进行了比较。