Issue 78, 2022

Engineered myoglobin as a catalyst for atom transfer radical cyclisation

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.

Graphical abstract: Engineered myoglobin as a catalyst for atom transfer radical cyclisation

Supplementary files

Article information

Article type
Communication
Submitted
08 jun 2022
Accepted
30 aug 2022
First published
31 aug 2022
This article is Open Access
Creative Commons BY license

Chem. Commun., 2022,58, 10989-10992

Engineered myoglobin as a catalyst for atom transfer radical cyclisation

A. Lubskyy, C. Guo, R. J. Chadwick, A. Petri-Fink, N. Bruns and M. M. Pellizzoni, Chem. Commun., 2022, 58, 10989 DOI: 10.1039/D2CC03227A

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