Light-driven decarboxylative deuteration enabled by a divergently engineered photodecarboxylase

Jian Xu (), Jiajie Fan, Yujiao Lou, Weihua Xu, Zhiguo Wang, Danyang Li, Haonan Zhou, Xianfu Lin and Qi Wu ()
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Jian Xu: Zhejiang University
Jiajie Fan: Zhejiang University
Yujiao Lou: Zhejiang University
Weihua Xu: Zhejiang University
Zhiguo Wang: Hangzhou Normal University
Danyang Li: Zhejiang University
Haonan Zhou: Zhejiang University
Xianfu Lin: Zhejiang University
Qi Wu: Zhejiang University

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Despite the well-established chemical processes for C-D bond formation, the toolbox of enzymatic methodologies for deuterium incorporation has remained underdeveloped. Here we describe a photodecarboxylase from Chlorella variabilis NC64A (CvFAP)-catalyzed approach for the decarboxylative deuteration of various carboxylic acids by employing D2O as a cheap and readily available deuterium source. Divergent protein engineering of WT-CvFAP is implemented using Focused Rational Iterative Site-specific Mutagenesis (FRISM) as a strategy for expanding the substrate scope. Using specific mutants, several series of substrates including different chain length acids, racemic substrates as well as bulky cyclic acids are successfully converted into the deuterated products (>40 examples). In many cases WT-CvFAP fails completely. This approach also enables the enantiocomplementary kinetic resolution of racemic acids to afford chiral deuterated products, which can hardly be accomplished by existing methods. MD simulations explain the results of improved catalytic activity and stereoselectivity of WT CvFAP and mutants.

Date: 2021
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DOI: 10.1038/s41467-021-24259-6

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