Engineered myoglobin as a catalyst for atom transfer radical cyclisation.
Andriy LubskyyChao GuoRobert J ChadwickAlke Petri-FinkNico BrunsMichela M PellizzoniPublished in: Chemical communications (Cambridge, England) (2022)
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.
Keyphrases
- electron transfer
- wild type
- molecular dynamics
- room temperature
- ionic liquid
- induced apoptosis
- highly efficient
- reduced graphene oxide
- crispr cas
- single cell
- cell cycle arrest
- metal organic framework
- cell therapy
- gold nanoparticles
- oxidative stress
- small molecule
- endoplasmic reticulum stress
- protein kinase
- signaling pathway
- binding protein