Froud R J, Ragan C I
Biochem J. 1984 Jan 15;217(2):551-60. doi: 10.1042/bj2170551.
Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely diffusible pool on the membrane. This model was based on that of Kröger & Klingenberg [(1973) Eur. J. Biochem. 34, 358-368] for ubiquinone-pool behaviour. Further confirmation of the pool model was provided by analysis of ubiquinol oxidase activity as a function of the molar ratio of the complexes and prediction of the degree of inhibition by antimycin.
泛醇氧化酶已由泛醇 - 细胞色素c还原酶(复合体III)、细胞色素c和细胞色素c氧化酶(复合体IV)重构而成。泛醇 - 2对细胞色素c的稳态还原水平随复合体的摩尔比以及抗霉素的存在而变化,这种变化方式可以通过一个模型进行定量解释,在该模型中细胞色素c作为膜上自由扩散的库起作用。这个模型是基于Kröger和Klingenberg [(1973年)《欧洲生物化学杂志》34卷,358 - 368页]关于泛醌库行为的模型。通过分析泛醇氧化酶活性作为复合体摩尔比的函数以及预测抗霉素的抑制程度,进一步证实了库模型。