Cupin Variants as Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes

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Cupin variants H52A and H54A/H58A effectively catalyzed stereoselective Michael addition of nitroalkanes, with C106N and F104W mutations further improving stereoselectivity and inverting diastereoselectivity.

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Abstract

Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantio-selective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, in silico substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.

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europepmc
last seen: 2026-05-19T01:45:01.086888+00:00