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<p>Haem peroxygenases are attractive biocatalysts for incorporating oxygen into organic molecules using H<sub>2</sub>O<sub>2</sub>. However, their practical applications are hindered by irreversible oxidative inactivation due to exogenous H<sub>2</sub>O<sub>2</sub> usage. Here we present an alternative catalytic route in haem peroxygenases that uses O<sub>2</sub> and small-molecule reductants such as ascorbic acid and dehydroascorbic acid (DHA) to drive reactions. Our experimental and computational studies indicated that DHAA, the hydrated form of DHA, serves as the key co-substrate that activates oxygen to generate the active oxyferryl haem compound I. We also demonstrate the broad applicability of this O<sub>2</sub>/reductant-dependent route across various haem peroxygenases, highlighting its biological significance for mono-oxygenase functionality. Importantly, this innovative route avoids the use of H<sub>2</sub>O<sub>2</sub>, thereby preventing the risk of irreversible enzyme inactivation. Finally, scaled-up reactions yielded chiral, value-added products with excellent productivity, underscoring the synthetic potential of this developed peroxygenase technology for sustainable chemical transformations.</p><p></p>

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An efficient catalytic route in haem peroxygenases mediated by O2/small-molecule reductant pairs for sustainable applications

  • 期刊论文

  • 发表日期：

    2025年1月28日

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  • Di Deng,
  • Zhihui Jiang,
  • Lixin Kang,
  • Langxing Liao,
  • Xiaodong Zhang,
  • Yuben Qiao,
  • Yang Zhou,
  • Liulin Yang,
  • Binju Wang,
  • Aitao Li

摘要

Haem peroxygenases are attractive biocatalysts for incorporating oxygen into organic molecules using H2O2. However, their practical applications are hindered by irreversible oxidative inactivation due to exogenous H2O2 usage. Here we present an alternative catalytic route in haem peroxygenases that uses O2 and small-molecule reductants such as ascorbic acid and dehydroascorbic acid (DHA) to drive reactions. Our experimental and computational studies indicated that DHAA, the hydrated form of DHA, serves as the key co-substrate that activates oxygen to generate the active oxyferryl haem compound I. We also demonstrate the broad applicability of this O2/reductant-dependent route across various haem peroxygenases, highlighting its biological significance for mono-oxygenase functionality. Importantly, this innovative route avoids the use of H2O2, thereby preventing the risk of irreversible enzyme inactivation. Finally, scaled-up reactions yielded chiral, value-added products with excellent productivity, underscoring the synthetic potential of this developed peroxygenase technology for sustainable chemical transformations.