化学
生物物理学
连接器
基质(水族馆)
电子转移
催化作用
构象变化
动力学
生物合成
血红素
蛋白质工程
细胞色素P450
蛋白质结构
立体化学
酶动力学
生物化学
嵌合体(遗传学)
蛋白质折叠
氧化还原酶
底物特异性
构象熵
细胞色素
折叠(DSP实现)
新陈代谢
作者
Ziqi Liang,Xitong Song,Shuming Cheng,Yiwen Shen,Jing Zhang,Yaru Wang,Huiying Luo,Bin Yao,Binju Wang,Tao Tu
标识
DOI:10.1002/advs.202519381
摘要
ABSTRACT Electron transfer (ET) efficiency dictates catalytic performance in multi‐domain self‐sufficient cytochrome P450s. Conventional engineering, however, predominantly focuses on localized optimization of either the active‐site pocket or linker regions, overlooking inter‐domain conformational transitions and ET chain integrity. Herein, we report a holistic ET‐optimization strategy integrating conformational dynamics modulation, ET pathway engineering, and substrate positioning tuning, which was applied to enhance ET in a chimeric P450 VK1‐CYP116B46‐L21 (L21) for calcifediol biosynthesis. [2Fe‐2S]→Heme ET pathway engineering yielded variant L21‐M2 (F346K/R354M), which decreased the conformational transition barrier by 4.5 kcal/mol and shortened the ET pathway by 4.05 Å, leading to a 72‐fold enhancement in ET rate. Heme domain engineering generated variant L21‐M3 (P83A/A177M/K180F), which shortened the near‐attack conformations distance to 4.19 Å (from 4.62 Å) and increased reactive conformation to 38 % (from 25 %). The pentuple variant L21‐M5 combined both improvements, which demonstrated exceptional catalytic performance: an 8.2‐ fold higher catalytic efficiency, a coupling efficiency of 56.78 %, and a total turnover number (TTN) of 3222. In a semi‐preparative‐scale biotransformation, L21‐M5 achieved 3.26 g/L production of calcifediol with 82 % conversion, underscoring its strong industrial potential. These results highlight the efficacy of the proposed ET‐optimization strategy and provide a transferable workflow for engineering multi‐domain redox biocatalysts.
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