Engineered myoglobin as a catalyst for atom transfer radical cyclisation

Andriy Lubskyy, Chao Guo, Robert J. Chadwick, Alke Petri-Fink, Nico Bruns, Michela M. Pellizzoni

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Myoglobin was subjected to site-directed mutagenesis and transformed into a catalyst able to perform atom transfer radical cyclisation reactions, i.e. intramolecular atom transfer radical additions. Replacing the iron-coordinating histidine with serine, or introducing small changes inside or at the entrance of the active site, transformed the completely inactive wild-type myoglobin into an artificial metalloenzyme able to catalyse the 5-exo cyclisation of halogenated unsaturated compounds for the synthesis of γ-lactams. This new-to-nature activity was achieved not only with purified protein but also in crude cell lysate and in whole cells.
Original languageEnglish
Pages (from-to)10989-10992
Number of pages4
JournalChemical Communications
Issue number78
Early online date31 Aug 2022
Publication statusPublished - 31 Aug 2022


  • materials chemistry
  • metals and alloys
  • surfaces, coatings and films
  • general chemistry
  • ceramics and composites
  • electronic, optical and magnetic materials
  • catalysis


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