Dolman D, Newell G A, Thurlow M D
Can J Biochem. 1975 May;53(5):495-501. doi: 10.1139/o75-069.
A kinetic study has been carried out over the pH range of 2.63-9.37 for the reaction of horseradish peroxidase with hydrogen peroxide to form compound I of th;e enzyme. Analysis of the results, indicates that there are two kinetic influencing, ionizable groups on the enzyme with pKa values of 3.2 and 3.9. Protonation of these groups results in a decrease in the rate of reaction of the enzyme with H2O2. A previous study of the kinetics of cyanide binding to horseradish peroxidase (Ellis, W.D. & Dunford, H.B.: Biochemistry 7, 2054-2062 (1968)) has been extended to down to pH 2.55, and analysis of these results also indicates the presence of two kinetically important ionizable groups on the enzyme with pKa values of 2.9 and 3.9.
对辣根过氧化物酶与过氧化氢反应生成该酶的化合物I的反应,在pH值2.63 - 9.37范围内进行了动力学研究。结果分析表明,该酶上有两个对动力学有影响的可电离基团,其pKa值分别为3.2和3.9。这些基团的质子化导致酶与H2O2反应速率降低。先前对氰化物与辣根过氧化物酶结合动力学的研究(埃利斯,W.D. & 邓福德,H.B.:《生物化学》7, 2054 - 2062 (1968))已扩展至pH值低至2.55,对这些结果的分析也表明该酶上存在两个对动力学重要的可电离基团,其pKa值分别为2.9和3.9。