Brittain T, Greenwood C
Department of Biochemistry, University of Auckland, New Zealand.
J Inorg Biochem. 1992 Oct 1;48(1):71-7. doi: 10.1016/0162-0134(92)80055-z.
Reduced azurin reacts with the resting, oxidized cytochrome c peroxidase of Pseudomonas aeruginosa to yield time courses observed at 420 nm, which consist of the sum of two exponential processes. Each process exhibits a hyperbolic dependence of the observed rate constant on the reduced azurin concentration. The fraction of the total optical density change which each process contributes is found to be dependent on the reduced azurin concentration. This pattern of reactivity is maintained at pH values between 5.5 and 8.0. The data has been analyzed in terms of a complex formation between the two proteins followed by an intramolecular electron exchange reaction. This analysis yields values for the binding constants at each pH value. The intramolecular exchange reaction is independent of pH, whilst the pH dependence of the binding reaction suggests the involvement of a histidine residue in this process.
还原型天青蛋白与铜绿假单胞菌处于静息态的氧化型细胞色素c过氧化物酶反应，产生在420nm处观察到的时间进程，该进程由两个指数过程之和组成。每个过程的观测速率常数对还原型天青蛋白浓度呈双曲线依赖关系。发现每个过程对总光密度变化的贡献比例取决于还原型天青蛋白浓度。在pH值5.5至8.0之间，这种反应模式保持不变。已根据两种蛋白质之间形成复合物并随后发生分子内电子交换反应对数据进行了分析。该分析得出了每个pH值下的结合常数。分子内交换反应与pH无关，而结合反应对pH的依赖性表明在此过程中有组氨酸残基参与。
