Brunori M, Parr S R, Greenwood C, Wilson M T
Biochem J. 1975 Oct;151(1):185-8. doi: 10.1042/bj1510185.
The electron-transfer reaction between azurin and the cytochrome oxidase from Pseudomonas aeruginosa was investigated by temperature-jump relaxation in the absence of O2 and in the presence of CO. The results show that: (i) reduced azurin exists in two forms in equilibrium, only one of which is capable of exchanging electrons with the Pseudomonas cytochrome oxidase, in agreement with M. T. Wilson, C. Greenwood, M. Brunori & E. Antonini (1975) (Biochem. J. 145, 449-457); (ii) the electron transfer between azurin and Pseudomonas cytochrome oxidase occurs within a molecular complex of the two proteins; this internal transfer becomes rate-limiting at high reagent concentrations.
在无氧和有一氧化碳存在的情况下,通过温度跃变弛豫法研究了天青蛋白与铜绿假单胞菌细胞色素氧化酶之间的电子转移反应。结果表明:(i)还原型天青蛋白以两种平衡形式存在,其中只有一种能够与铜绿假单胞菌细胞色素氧化酶交换电子,这与M. T. 威尔逊、C. 格林伍德、M. 布鲁诺里和E. 安东尼尼(1975年)(《生物化学杂志》145卷,449 - 457页)的研究结果一致;(ii)天青蛋白与铜绿假单胞菌细胞色素氧化酶之间的电子转移发生在两种蛋白质的分子复合物内;在高试剂浓度下,这种内部转移成为限速步骤。