Light-Driven Deracemization by a Designed Photoenzyme

The creation of enzymes with abiological abilities offers exciting opportunities to access new-to-nature biocatalysis beyond that found in nature. Here, we repurpose a novel protein scaffold, CTB10, as an artificial photoenzyme through genetic code expansion. It enables catalytic deracemization of cyclopropane, a process that remains inaccessible to traditional biocatalysis due to its thermodynamically unfavorable nature. Following structural optimization through directed evolution, a broad substrate scope with high enantioselectivities is achieved. Furthermore, the crystal structure of the CTB10-based photoenzyme-substrate complex well demonstrates how the catalytic chiral cavity is sculpted to promote efficient and selective light-enabled deracemization. Therefore, this study unlocks the potential for achieving challenging deracemization through biocatalysis.

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Publication Details

Journal
Journal of the American Chemical Society
Published
2025-04-12
DOI
https://doi.org/10.1021/jacs.4c16521
Citations
20
Primary Topic
Radical Photochemical Reactions
Type
article
Field-Weighted Citation Impact
18.72
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article

Light-Driven Deracemization by a Designed Photoenzyme

Kai Fu, Zhiwei Deng, Yijian Rao, Zhenbo Yuan et al.
20 citations
Journal of the American Chemical Society
Radical Photochemical Reactions
18.72
article

Light-Driven Deracemization by a Designed Photoenzyme

Kai Fu, Zhiwei Deng, Yijian Rao, Zhenbo Yuan, Zhengshan Luo, Min Li, Yan Zhang
article en
20 citations

Abstract

The creation of enzymes with abiological abilities offers exciting opportunities to access new-to-nature biocatalysis beyond that found in nature. Here, we repurpose a novel protein scaffold, CTB10, as an artificial photoenzyme through genetic code expansion. It enables catalytic deracemization of cyclopropane, a process that remains inaccessible to traditional biocatalysis due to its thermodynamically unfavorable nature. Following structural optimization through directed evolution, a broad substrate scope with high enantioselectivities is achieved. Furthermore, the crystal structure of the CTB10-based photoenzyme-substrate complex well demonstrates how the catalytic chiral cavity is sculpted to promote efficient and selective light-enabled deracemization. Therefore, this study unlocks the potential for achieving challenging deracemization through biocatalysis.

Journal of the American Chemical SocietyVol. 147(16)
Jiangnan University (CN)
Openalex Percentile: Top 0%
Radical Photochemical Reactions
18.72
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