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<p>Methods for direct enantioselective oxidation of C(<i>sp</i><sup>3</sup>)–H bonds will revolutionize the preparation of chiral alcohols and their derivatives. Enzymatic catalysis, which uses key metal-oxo species to facilitate efficient hydrogen atom abstraction, has evolved as a highly selective approach for C–H oxidation in biological systems. Despite its effectiveness, reproducing this function and achieving high stereoselectivity in biomimetic catalysts has proven to be a daunting task. Here we present a copper-based biomimetic catalytic system that achieves highly efficient asymmetric <i>sp</i><sup>3</sup> C–H oxidation with C–H substrates as the limiting reagent. A Cu(II)-bound <i>tert</i>-butoxy radical is responsible for the site-selective C–H bond cleavage, which resembles the active site of copper-based enzymes for C–H oxidation. The developed method has been successfully accomplished with good functional group compatibility and exceptionally high site- and enantioselectivity, which is applicable for the late-stage oxidation of bioactive compounds.</p><p></p>

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Site- and enantioselective allylic and propargylic C–H oxidation enabled by copper-based biomimetic catalysis

  • 期刊论文

  • 发表日期：

    2025年1月8日

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  • Honggang Zhang,
  • Yibo Zhou,
  • Tilong Yang,
  • Jingui Wu,
  • Pinhong Chen,
  • Zhenyang Lin,
  • Guosheng Liu

摘要

Methods for direct enantioselective oxidation of C(sp3)–H bonds will revolutionize the preparation of chiral alcohols and their derivatives. Enzymatic catalysis, which uses key metal-oxo species to facilitate efficient hydrogen atom abstraction, has evolved as a highly selective approach for C–H oxidation in biological systems. Despite its effectiveness, reproducing this function and achieving high stereoselectivity in biomimetic catalysts has proven to be a daunting task. Here we present a copper-based biomimetic catalytic system that achieves highly efficient asymmetric sp3 C–H oxidation with C–H substrates as the limiting reagent. A Cu(II)-bound tert-butoxy radical is responsible for the site-selective C–H bond cleavage, which resembles the active site of copper-based enzymes for C–H oxidation. The developed method has been successfully accomplished with good functional group compatibility and exceptionally high site- and enantioselectivity, which is applicable for the late-stage oxidation of bioactive compounds.