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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.

SUBMITTER: Lubskyy A 

PROVIDER: S-EPMC9521412 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Engineered myoglobin as a catalyst for atom transfer radical cyclisation.

Lubskyy Andriy A   Guo Chao C   Chadwick Robert J RJ   Petri-Fink Alke A   Bruns Nico N   Pellizzoni Michela M MM  

Chemical communications (Cambridge, England) 20220929 78


Myoglobin was subjected to site-directed mutagenesis and transformed into a catalyst able to perform atom transfer radical cyclisation reactions, <i>i.e</i>. 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-<i>exo</i> cyclisation of halogenated unsaturated co  ...[more]

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