Rönnberg M, Ellfolk N
Acta Chem Scand B. 1975;29(7):719-27. doi: 10.3891/acta.chem.scand.29b-0719.
The steady state kinetics of cytochrome c peroxidase from Pseudomonas aeruginosa (PaCCP) has been studied by initial velocity techniques using several cytochromes c (550 and 555 P. aeruginosa; 551 P. fluorescens) and Pseudomonas azurin as electron donors and hydrogen peroxide as electron acceptor. From the initial velocity patterns a sequential mechanism with compulsory substrate-binding order is proposed for PaCCP. A comparative kinetic study of the peroxidatic oxidation of cytochrome c-551 (P. aeruginosa) by yeast cytochrome c peroxidase was made to evaluate the significance of electrostatic interactions in complex formation between the enzyme and substrates.
利用初始速度技术，以几种细胞色素c（铜绿假单胞菌的细胞色素c550和555；荧光假单胞菌的细胞色素c551）和铜绿假单胞菌蓝蛋白作为电子供体，过氧化氢作为电子受体，对铜绿假单胞菌细胞色素c过氧化物酶（PaCCP）的稳态动力学进行了研究。根据初始速度模式，提出了PaCCP具有强制底物结合顺序的序列机制。对酵母细胞色素c过氧化物酶催化细胞色素c-551（铜绿假单胞菌）的过氧化物氧化进行了比较动力学研究，以评估静电相互作用在酶与底物复合物形成中的重要性。
