This research demonstrates the effective use of apo-myoglobin and organocatalytic cofactor for ketone reactions, suggesting new pathways for enzyme evolution.
Current research on artificial aldolases predominantly centers on aldehyde substrates with relatively limited exploration of ketone substrates. Here, we report the creation of a novel artificial aldolase based on apo-myoglobin by embedding an organocatalytic secondary amine cofactor in the protein's distal pocket. The designer enzyme exhibits good to excellent enantioselectivities (up to 97.5:2.5 er) for couplings of acetone with diverse aldehyde substrates. This work establishes apo-myoglobin as a versatile chassis for integrating abiological organocatalysts and demonstrates that combining non-natural cofactors with directed evolution can unlock C-C bond-forming reactivities.
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Hu et al. (2025) studied this question.
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