Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of Korea.
J Am Chem Soc. 2023 Mar 8;145(9):5211-5221. doi: 10.1021/jacs.2c12226. Epub 2023 Feb 24.
Efficient and environmentally friendly conversion of light energy for direct utilization in chemical production has been a long-standing goal in enzyme design. Herein, we synthesized artificial photocatalytic enzymes by introducing an Ir photocatalyst and a Ni(bpy) complex to an optimal protein scaffold in close proximity. Consequently, the enzyme generated C-O coupling products with up to 96% yields by harvesting visible light and performing intramolecular electron transfer between the two catalysts. We systematically modulated the catalytic activities of the artificial photocatalytic cross-coupling enzymes by tuning the electrochemical properties of the catalytic components, their positions, and distances within a protein. As a result, we discovered the best-performing mutant that showed broad substrate scopes under optimized conditions. This work explicitly demonstrated that we could integrate and control both the inorganic and biochemical components of photocatalytic biocatalysis to achieve high yield and selectivity in valuable chemical transformations.
高效、环保地将光能转化为直接用于化学生产的能源，一直是酶设计的长期目标。在此，我们通过在最佳蛋白质支架中引入 Ir 光催化剂和 Ni(bpy) 配合物，合成了人工光催化酶。由此，该酶通过收集可见光并在两个催化剂之间进行分子内电子转移，生成 C-O 偶联产物，产率高达 96%。我们通过调节催化组件的电化学性质、它们在蛋白质中的位置和距离，系统地调节人工光催化交叉偶联酶的催化活性。结果，我们发现了表现最佳的突变体，在优化条件下显示出广泛的底物范围。这项工作明确表明，我们可以整合和控制光催化生物催化中的无机和生化组件，以在有价值的化学转化中实现高产率和高选择性。
