Rönnberg M
Acta Chem Scand B. 1976;30(8):721-6. doi: 10.3891/acta.chem.scand.30b-0721.
Kinetic studies of the reaction mechanism of Pseudomonas cytochrome c peroxidase (PaCCP) were made by the method of product inhibition using oxidized cytochrome C (551 P.aeruginosa) and oxidized Pseudomonas azurin as products. Inhibition by the two oxidized substrates was linearly non-competitive towards the respective reduced electron donor and towards hydrogen peroxide. Although a full kinetic analysis is experimentally impossible in a peroxidase-type reaction, the results do provide some evidence in favour of an ordered reaction mechanism in which hydrogen peroxide is the first to add to PaCCP and electron donor the second.
利用氧化型细胞色素C(铜绿假单胞菌551)和氧化型铜绿假单胞菌天青蛋白作为产物,通过产物抑制法对铜绿假单胞菌细胞色素c过氧化物酶(PaCCP)的反应机制进行了动力学研究。两种氧化型底物的抑制作用对各自的还原型电子供体和过氧化氢呈线性非竞争性。虽然在过氧化物酶型反应中进行完整的动力学分析在实验上是不可能的,但这些结果确实提供了一些证据,支持一种有序的反应机制,其中过氧化氢首先添加到PaCCP,电子供体其次。