Engineered myoglobin as a catalyst for atom transfer radical cyclisation

Lubskyy, Andriy and Guo, Chao and Chadwick, Robert J. and Petri-Fink, Alke and Bruns, Nico and Pellizzoni, Michela M. (2022) Engineered myoglobin as a catalyst for atom transfer radical cyclisation. Chemical Communications, 58 (78). pp. 10989-10992. ISSN 1359-7345 (https://doi.org/10.1039/d2cc03227a)

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Abstract

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.

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