Whole-cell-catalyzed hydrogenation/deuteration of aryl halides with a genetically repurposed photodehalogenase
Whole-cell-catalyzed hydrogenation/deuteration of aryl halides with a genetically repurposed photodehalogenase
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DOI：
10.1016/j.chempr.2023.03.006
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发表时间：
2023-07-13
期刊：
影响因子：
23.5
通讯作者：
Zhong, Fangrui
中科院分区：
文献类型：
--
作者：
Fu, Yu;Liu, Xiaohong;Zhong, Fangrui
具有新的自然反应性的人工酶非常适合于扩大可持续合成的生物催化体系。为此，人工光酶嵌入了合成化学中建立的一种突出的光氧化还原催化剂，可以利用光能触发非生物底物的电子转移转化。在这里，我们证明了编码在黄色荧光蛋白中的二苯甲酮光催化剂(RPDase)可以很好地催化芳基卤化物的生物催化加氢脱卤化反应。与为特定底物的生物修复而进化的天然金属辅因子依赖的脱卤酶不同，这种不含金属的光合酶通过完全非自然的催化机制与甲酸盐结合工作，并表现出显著的底物通用性。利用RPDase的双正交性和遗传密码扩展方法，我们进一步展示了第一个利用表达RPDase的重组大肠杆菌细胞进行全细胞光生物催化的方法。我们的结果表明，含有人工合成有机光催化剂的人工酶有望为有价值的非生物反应产生非自然代谢。
Artificial enzymes with new-to-nature reactivity are highly desirable to expand the repertoire of biocatalysis for sustainable synthesis. To this end, artificial photoenzymes embedded with a prominent photoredox catalyst established in synthetic chemistry can harness light energy to trigger electron transfer transformations of abiological substrates. Herein, we demonstrate that a benzophenone photocatalyst encoded in a yellow fluorescent protein named reductive photodehalogenase (RPDase) can proficiently mediate the biocatalytic hydrodehalogenation and deuterodehalogenation of aryl halides. Unlike natural metal-cofactor-dependent dehalogenases evolved for the bioremediation of specific substrates, this metal-free photo enzyme operates in combination with formate via an entirely unnatural catalytic mechanism and exhibits marked substrate generality. Taking advantage of the biorthogonality of RPDase and the genetic code expansion method, we further demonstrated the first whole cell photobiocatalysis using recombinant Escherichia coli cells that express RPDase. Our results show that artificial enzymes bearing a synthetic organophotocatalyst is promising to generate a non -natural metabolism for valuable abiological reactions.