Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of Korea.
Inorg Chem. 2022 Aug 8;61(31):12433-12441. doi: 10.1021/acs.inorgchem.2c01898. Epub 2022 Jul 24.
Artificial metalloenzymes have fed our understanding of how inorganic reactivities emerge, evolve, and diversify in protein environments. Herein, we created dinuclear copper oxidases by genetically encoding a metal-ligating unnatural amino acid (bpy-Ala) per protomer in the vicinity of the innate C rotational axis of a homo-oligomeric protein. The inherent protein symmetry allows the precise multiplication and placement of two Cu(bpy) species. Depending on the location of bpy-Ala, the tailor-made metalloenzymes exhibited electronically uncoupled or coupled dicopper sites. Consequently, they displayed various reactivities with dioxygen associated with multiple protons and electrons, illustrating a diverse chemical repertoire of artificial copper-dependent enzymes.
人工金属酶使我们深入了解了无机反应性在蛋白质环境中是如何产生、演变和多样化的。在这里，我们通过在同源寡聚蛋白的固有 C 旋转轴附近每个亚基中遗传编码一个金属配体非天然氨基酸（bpy-Ala），构建了双核铜氧化酶。内在的蛋白质对称性允许两种 Cu(bpy) 物种的精确倍增和定位。根据 bpy-Ala 的位置，定制的金属酶表现出电子不耦合或耦合的双核铜位点。因此，它们与多种质子和电子相关的氧气表现出不同的反应性，展示了各种人工依赖铜的酶的化学多样性。
