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Engineered enzyme performs key synthetic reaction with near-perfect control | The study mark the first time an enzyme has been shown to catalyze this type of reaction, offering a new tool for greener, more selective chemical synthesis.
Cytochrome P450 enzymes can be repurposed to catalyse asymmetric metal–hydride hydrogen atom transfer, a new-to-nature reaction.
To complement heterolytic metal–hydride bond cleavage, metal–hydride hydrogen atom transfer (MHAT) has recently gained attention, as a promising strategy for radical hydrofunctionalization of unactivated alkenes 2, thus enabling late-stage diversification of complex molecules 3, 4. Directed evolution of P450 BM3 yielded a triple mutant that catalyses MHAT radical cyclization of unactivated alkenes, producing diverse cyclic compounds—including pyrrolidines and piperidines—with up to 98:2 enantiomeric ratio under aerobic whole-cell conditions. Kato, S., Abe, M., Gröger, H. & Hayashi, T. Reconstitution of myoglobin with iron porphycene generates an artificial aldoxime dehydratase with expanded catalytic activities.
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