IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-59176-5.html
   My bibliography  Save this article

Enantioselective dearomative ortho-cycloaddition transformation of unactivated arenes by cage-confined visible-light photocatalysis

Author

Listed:
  • Jie Yang

    (Sun Yat-Sen University)

  • Zhongshu Li

    (Sun Yat-Sen University)

  • Xiantao Wu

    (Sun Yat-Sen University)

  • Jie Chen

    (Sun Yat-Sen University)

  • Sisi Huang

    (Sun Yat-Sen University)

  • Yu-Lin Lu

    (Sun Yat-Sen University)

  • Zhiwei Jiao

    (Sun Yat-Sen University)

  • Cheng-Yong Su

    (Sun Yat-Sen University)

Abstract

Photoinduced dearomatization of arenes is a powerful strategy in organic synthesis to disrupt the stable aromaticity; however, the asymmetric dearomatization photocatalysis of unactivated arenes remains highly challenging and rare. Herein we demonstrate an enzyme-mimicking cage-confined visible-light asymmetric photocatalysis method for intramolecular dearomative cycloaddition with electron-deficient β-aryl enones. Owing to the multi-functional synergy of chirality, energy transfer, and host-guest interactions in the confined microenvironments, the self-assembled chiral cage-photoreactor could pre-organize the arenes and activate the β-aryl enones to give stereoselectively fused cyclobutanes through visible-light induced [2 + 2] ortho-cycloaddition. Notably, the competing transformation to stable [4 + 2] cycloadducts has been inhibited, producing thermodynamically unfavorable [2 + 2] cycloadducts with excellent regio-, diastereo-, and enantioselectivities.

Suggested Citation

  • Jie Yang & Zhongshu Li & Xiantao Wu & Jie Chen & Sisi Huang & Yu-Lin Lu & Zhiwei Jiao & Cheng-Yong Su, 2025. "Enantioselective dearomative ortho-cycloaddition transformation of unactivated arenes by cage-confined visible-light photocatalysis," Nature Communications, Nature, vol. 16(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59176-5
    DOI: 10.1038/s41467-025-59176-5
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-59176-5
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-59176-5?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Sarah L. Lovelock & Rebecca Crawshaw & Sophie Basler & Colin Levy & David Baker & Donald Hilvert & Anthony P. Green, 2022. "The road to fully programmable protein catalysis," Nature, Nature, vol. 606(7912), pages 49-58, June.
    2. Kai Wu & Kang Li & Ya-Jun Hou & Mei Pan & Lu-Yin Zhang & Ling Chen & Cheng-Yong Su, 2016. "Homochiral D4-symmetric metal–organic cages from stereogenic Ru(II) metalloligands for effective enantioseparation of atropisomeric molecules," Nature Communications, Nature, vol. 7(1), pages 1-10, April.
    3. Jonathan S. Trimble & Rebecca Crawshaw & Florence J. Hardy & Colin W. Levy & Murray J. B. Brown & Douglas E. Fuerst & Derren J. Heyes & Richard Obexer & Anthony P. Green, 2022. "A designed photoenzyme for enantioselective [2+2] cycloadditions," Nature, Nature, vol. 611(7937), pages 709-714, November.
    4. Ningning Sun & Jianjian Huang & Junyi Qian & Tai-Ping Zhou & Juan Guo & Langyu Tang & Wentao Zhang & Yaming Deng & Weining Zhao & Guojiao Wu & Rong-Zhen Liao & Xi Chen & Fangrui Zhong & Yuzhou Wu, 2022. "Enantioselective [2+2]-cycloadditions with triplet photoenzymes," Nature, Nature, vol. 611(7937), pages 715-720, November.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Haoran Huang & Tao Yan & Chang Liu & Yuxiang Lu & Zhigang Wu & Xingchu Wang & Jie Wang, 2024. "Genetically encoded Nδ-vinyl histidine for the evolution of enzyme catalytic center," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Meng-Fan Wang & Yun-Hu Deng & Yu-Xuan Hong & Jia-Hui Gu & Yong-Yong Cao & Qi Liu & Pierre Braunstein & Jian-Ping Lang, 2023. "In situ observation of a stepwise [2 + 2] photocycloaddition process using fluorescence spectroscopy," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    3. Amy E. Hutton & Jake Foster & Rebecca Crawshaw & Florence J. Hardy & Linus O. Johannissen & Thomas M. Lister & Emilie F. Gérard & Zachary Birch-Price & Richard Obexer & Sam Hay & Anthony P. Green, 2024. "A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Jianjian Huang & Tai-Ping Zhou & Ningning Sun & Huaibin Yu & Xixiang Yu & Rong-Zhen Liao & Weijun Yao & Zhifeng Dai & Guojiao Wu & Fangrui Zhong, 2024. "Accessing ladder-shape azetidine-fused indoline pentacycles through intermolecular regiodivergent aza-Paternò–Büchi reactions," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    5. Zi-Lin Li & Shuxin Pei & Ziying Chen & Teng-Yu Huang & Xu-Dong Wang & Lin Shen & Xuebo Chen & Qi-Qiang Wang & De-Xian Wang & Yu-Fei Ao, 2024. "Machine learning-assisted amidase-catalytic enantioselectivity prediction and rational design of variants for improving enantioselectivity," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    6. Jun-Kuan Li & Ge Qu & Xu Li & Yuchen Tian & Chengsen Cui & Fa-Guang Zhang & Wuyuan Zhang & Jun-An Ma & Manfred T. Reetz & Zhoutong Sun, 2022. "Rational enzyme design for enabling biocatalytic Baldwin cyclization and asymmetric synthesis of chiral heterocycles," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    7. Peihua Lin & Bo Zhang & Hongli Yang & Shengfei Yang & Pengpeng Xue & Ying Chen & Shiyi Yu & Jichao Zhang & Yixiao Zhang & Liwei Chen & Chunhai Fan & Fangyuan Li & Daishun Ling, 2024. "An artificial protein modulator reprogramming neuronal protein functions," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    8. Xudong Wang & Chris Neale & Soo-Kyung Kim & William A. Goddard & Libin Ye, 2023. "Intermediate-state-trapped mutants pinpoint G protein-coupled receptor conformational allostery," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    9. Enrico Orsi & Lennart Schada von Borzyskowski & Stephan Noack & Pablo I. Nikel & Steffen N. Lindner, 2024. "Automated in vivo enzyme engineering accelerates biocatalyst optimization," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    10. Thuy N. Nguyen & Christine Ingle & Samuel Thompson & Kimberly A. Reynolds, 2024. "The genetic landscape of a metabolic interaction," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59176-5. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.