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Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes
Auteur(s)
Skander, Myriem
Humbert, Nicolas
Collot, Jérôme
Gradinaru, Julieta
Klein, Gérard
Loosli, Andreas
Sauser, Jérôme
Zocchi, Andrea
Gilardoni, François
Ward, Thomas R.
Date de parution
2004
In
Journal of the American Chemical Society (JACS), American Chemical Society (ACS), 2004/126/44/14411–14418
Résumé
We report on the generation of artificial metalloenzymes based on the noncovalent incorporation of biotinylated rhodium−diphosphine complexes in (strept)avidin as host proteins. A chemogenetic optimization procedure allows one to optimize the enantioselectivity for the reduction of acetamidoacrylic acid (up to 96% ee (<i>R</i>) in streptavidin S112G and up to 80% ee (<i>S</i>) in WT avidin). The association constant between a prototypical cationic biotinylated rhodium−diphosphine catalyst precursor and the host proteins was determined at neutral pH: log <i>K</i><sub>a</sub> = 7.7 for avidin (pI = 10.4) and log <i>K</i><sub>a</sub> = 7.1 for streptavidin (pI = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 °C with a 1% catalyst loading.
Identifiants
Type de publication
journal article
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