Whole-cell-catalyzed hydrogenation/deuteration of aryl halides with a genetically repurposed photodehalogenase
Yu Fu, Xiaohong Liu, Yan Xia, Xuzhen Guo, Juan Guo, Junshuai Zhang, Weining Zhao, Yuzhou Wu, Jiangyun Wang, Fangrui Zhong
Abstract
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 photoenzyme 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.
附件下载：
Whole-cell-catalyzed hydrogenation/deuteration of aryl halides with a genetically repurposed photodehalogenase, Cell Chem, 5 April 2023
Cell Chem, 5 April, 2023, DOI：https://doi.org/10.1016/j.chempr.2023.03.006
Whole-cell-catalyzed hydrogenation/deuteration of aryl halides with a genetically repurposed photodehalogenase
Yu Fu, Xiaohong Liu, Yan Xia, Xuzhen Guo, Juan Guo, Junshuai Zhang, Weining Zhao, Yuzhou Wu, Jiangyun Wang, Fangrui Zhong
Abstract
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 photoenzyme 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.
文章链接：https://www.sciencedirect.com/science/article/abs/pii/S2451929423001250?via%3Dihub
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