Biocatalytic Asymmetric Radical Dearomatization of Electrophilic Heterocyclic and Non-Heterocyclic Arenes

Catalytic asymmetric dearomatization provides a powerful strategy for converting readily available aromatic feedstocks into valuable three-dimensional molecular scaffolds. Despite substantial advances over the past several decades, general methods for catalytic asymmetric dearomatization of electrophilic arenes, particularly non-heterocyclic substrates with high aromatic stabilization energies, remain a challenging task. Here, we report the use of a hydrogen atom transfer mechanism for biocatalytic radical dearomatization of electron-deficient arenes. Repurposing and directed evolution of our previously developed P450 halogen atom transferases furnished hydrogen atom transfer dearomatases that catalyze the stereoselective dearomatization of a range of electrophilic arenes, including electron-deficient indoles, pyrroles, and simple benzene derivatives. These evolved biocatalysts facilitated both diastereodivergent and enantiodivergent radical dearomatization, providing access to fused and spirocyclic chiral scaffolds bearing challenging quaternary and/or contiguous stereocenters. Computational and experimental studies revealed that a strategically positioned active-site lysine residue enables enzyme-controlled proton transfer against the intrinsic thermodynamic stereopreference, allowing catalyst-controlled reversal of diastereoselectivity from a common radical intermediate. Importantly, the evolved dearomatases efficiently transformed challenging arene substrates that proved recalcitrant under previously optimized Fe, Mn and Co-based metal-hydride hydrogen atom transfer conditions. Collectively, these results establish new-to-nature metalloredox biocatalysis as a powerful strategy for overcoming longstanding challenges in asymmetric radical catalysis.

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Publication Details

Journal
bioRxiv (Cold Spring Harbor Laboratory)
Published
2026-11-09
DOI
https://doi.org/10.64898/2026.11.07.764688
Primary Topic
Enzyme Catalysis and Immobilization
Type
preprint
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preprint

Biocatalytic Asymmetric Radical Dearomatization of Electrophilic Heterocyclic and Non-Heterocyclic Arenes

Pei‐Pei Xie, Peng Liu, Hong Chen, Heyu Chen et al.
bioRxiv (Cold Spring Harbor Laboratory)
Enzyme Catalysis and Immobilization
preprint

Biocatalytic Asymmetric Radical Dearomatization of Electrophilic Heterocyclic and Non-Heterocyclic Arenes

Pei‐Pei Xie, Peng Liu, Hong Chen, Heyu Chen, Yu Tian, Ken Lin, Yang Yang
preprint en

Abstract

Catalytic asymmetric dearomatization provides a powerful strategy for converting readily available aromatic feedstocks into valuable three-dimensional molecular scaffolds. Despite substantial advances over the past several decades, general methods for catalytic asymmetric dearomatization of electrophilic arenes, particularly non-heterocyclic substrates with high aromatic stabilization energies, remain a challenging task. Here, we report the use of a hydrogen atom transfer mechanism for biocatalytic radical dearomatization of electron-deficient arenes. Repurposing and directed evolution of our previously developed P450 halogen atom transferases furnished hydrogen atom transfer dearomatases that catalyze the stereoselective dearomatization of a range of electrophilic arenes, including electron-deficient indoles, pyrroles, and simple benzene derivatives. These evolved biocatalysts facilitated both diastereodivergent and enantiodivergent radical dearomatization, providing access to fused and spirocyclic chiral scaffolds bearing challenging quaternary and/or contiguous stereocenters. Computational and experimental studies revealed that a strategically positioned active-site lysine residue enables enzyme-controlled proton transfer against the intrinsic thermodynamic stereopreference, allowing catalyst-controlled reversal of diastereoselectivity from a common radical intermediate. Importantly, the evolved dearomatases efficiently transformed challenging arene substrates that proved recalcitrant under previously optimized Fe, Mn and Co-based metal-hydride hydrogen atom transfer conditions. Collectively, these results establish new-to-nature metalloredox biocatalysis as a powerful strategy for overcoming longstanding challenges in asymmetric radical catalysis.

bioRxiv (Cold Spring Harbor Laboratory)
University of California, Santa Barbara (US), University of Pittsburgh (US)
Enzyme Catalysis and Immobilization
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