Engineered myoglobin as a catalyst for atom transfer radical cyclisation

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 gamma-lactams. This new-to-nature activity was achieved not only with purified protein but also in crude cell lysate and in whole cells.

Automated summary

By mutating the protein, wild-type myoglobin was transformed into an artificial metalloenzyme capable of catalyzing the cyclization reaction of halogenated unsaturated compounds for the synthesis of gamma-lactams. This new activity was achieved not only in purified protein, but also in crude cell lysate and in whole cells.