细胞色素P450分布于物种进化的各谱系内，通过催化内、外源底物的氧化反应发挥重要生理功能，该反应需要其氧化还原搭档POR提供不可或缺的电子。与P450种类多样性截然不同，POR以单拷贝存在于昆虫基因组，并向不同P450提供电子，成为P450催化活性的限速因子。目前，昆虫体内单一结构的POR分子能与不同P450互作并传递电子的结构机理仍不清楚。为此，本研究以德国小蠊P450酶系为研究对象，通过进化印记分析预测POR分子中与P450发生功能性互作的关键氨基酸位点，并用定点突变与异源活性表达技术验证这些位点构成的柔性表面在二者互作过程中的作用，进而阐明细胞色素P450与POR发生功能互作的分子机理。

Cytochrome P450s exist in all the phylogenetic clades of biological world and play important biological roles by catalyzing aerobic oxidation of many endogenous and exogenous substrates, which depends on the electrons provided by cytochrome P450 oxidoreductase (POR). In contrast to the diversity of P450 type, POR with a single copy exists in the genome of insect. So POR is the key rate-limiting factor to P450 activities. The molecular mechanisms that one POR can interact with various P450s have not been clearly characterized so far. This study attempts to predict the key amino acid sites involved in functional interaction between P450-POR in German cockroach by virtue of evolutionary trace analysis and validate the function of key residues by utilizing site-directed mutagenesis and biochemical activity analysis.