Electroenzymatic Oxidative Desymmetrization by Engineered Thiamine-Dependent Enzymes for the Enantioselective Synthesis of Axially Chiral Biaryls

While biocatalysis and electrochemistry each offer unique advantages, such as enzyme selectivity and traceless electron use, their integration for unlocking new enzyme function remains limited. Here, we report a new-to-nature electroenzymatic desymmetrization strategy that enables the enantiodivergent synthesis of biaryls bearing axial chirality. By synergistically combining protein engineering and mediated electrolysis, we repurpose thiamine-dependent enzymes for the highly efficient biocatalytic desymmetrization of biaryl dialdehydes, achieving high enantioselectivity (up to >99% e.e., with enantiodivergence accessible in some cases), excellent yield (up to 99%), and low enzyme loading (down to 0.1 mol %, up to 930 TON). Mechanistic investigations confirm that electrochemically generated enzyme-bound radicals are key to this unnatural reactivity, and the engineered protein scaffolds provide precise enantiodiscrimination while preventing detrimental overoxidation. This work showcases the potential of synergistic electroenzymatic synthesis as a powerful platform for unlocking new enzyme reactivity, offering a compelling alternative to established methods such as photobiocatalysis and artificial enzymes.

Authors

Institutions

Publication Details

Journal
Journal of the American Chemical Society
Published
2026-05-17
DOI
https://doi.org/10.1021/jacs.6c01275
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Electroenzymatic Oxidative Desymmetrization by Engineered Thiamine-Dependent Enzymes for the Enantioselective Synthesis of Axially Chiral Biaryls

Jianmin Wu, Xiaoqiang Huang, Aokun Liu, Fengming Shi et al.
Journal of the American Chemical Society
Enzyme Catalysis and Immobilization
article

Electroenzymatic Oxidative Desymmetrization by Engineered Thiamine-Dependent Enzymes for the Enantioselective Synthesis of Axially Chiral Biaryls

Jianmin Wu, Xiaoqiang Huang, Aokun Liu, Fengming Shi, Yingzhi Ren, L J Yu, Yuanzhang Zhao, Beibei Zhao, Jinhai Yu, Bin Chen, Yan Zhang
article en

Abstract

While biocatalysis and electrochemistry each offer unique advantages, such as enzyme selectivity and traceless electron use, their integration for unlocking new enzyme function remains limited. Here, we report a new-to-nature electroenzymatic desymmetrization strategy that enables the enantiodivergent synthesis of biaryls bearing axial chirality. By synergistically combining protein engineering and mediated electrolysis, we repurpose thiamine-dependent enzymes for the highly efficient biocatalytic desymmetrization of biaryl dialdehydes, achieving high enantioselectivity (up to >99% e.e., with enantiodivergence accessible in some cases), excellent yield (up to 99%), and low enzyme loading (down to 0.1 mol %, up to 930 TON). Mechanistic investigations confirm that electrochemically generated enzyme-bound radicals are key to this unnatural reactivity, and the engineered protein scaffolds provide precise enantiodiscrimination while preventing detrimental overoxidation. This work showcases the potential of synergistic electroenzymatic synthesis as a powerful platform for unlocking new enzyme reactivity, offering a compelling alternative to established methods such as photobiocatalysis and artificial enzymes.

Journal of the American Chemical Society
University of Science and Technology of China (CN), State Key Laboratory of Chemical Engineering (CN), Nanjing University (CN)
Reduced inequalities, Peace, Justice and strong institutions
Openalex Percentile: Top 8%
Enzyme Catalysis and Immobilization
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.