AI Article Synopsis

  • The study introduces CoNSA-POase, an artificial peroxygenase made from single-atom cobalt supported on polymeric carbon nitrogen, which shows excellent performance in converting aromatic alkanes to ketones.
  • Density functional theory indicates that this artificial enzyme operates via a different catalytic mechanism compared to natural peroxygenases.
  • The integration of CoNSA-POase with other enzymes in continuous-flow systems enhances the efficient production of chiral alcohols and amines, suggesting potential advancements in enzyme-based applications.

Article Abstract

We report the synthesis and characterization of an artificial peroxygenase (CoNSA-POase) with CoN active sites by supporting single-atom cobalt on polymeric carbon nitrogen, which exhibits high activity, selectivity, stability, and reusability in the oxidation of aromatic alkanes to ketones. Density functional theory calculations reveal a different catalytic mechanism for the artificial peroxygenase from that of natural peroxygenases. In addition, continuous-flow systems are employed to combine CoNSA-POase with enantiocomplementary ketoreductases as well as an amine dehydrogenase, enabling the enantioselective synthesis of chiral alcohols and amines from hydrocarbons with significantly improved productivity. This work, emulating nature and beyond nature, provides a promising design concept for heme enzyme-based transformations.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11629291PMC
http://dx.doi.org/10.1021/acscatal.4c03161DOI Listing

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Article Synopsis
  • The study introduces CoNSA-POase, an artificial peroxygenase made from single-atom cobalt supported on polymeric carbon nitrogen, which shows excellent performance in converting aromatic alkanes to ketones.
  • Density functional theory indicates that this artificial enzyme operates via a different catalytic mechanism compared to natural peroxygenases.
  • The integration of CoNSA-POase with other enzymes in continuous-flow systems enhances the efficient production of chiral alcohols and amines, suggesting potential advancements in enzyme-based applications.
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