Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes
Citations Over TimeTop 10% of 2004 papers
Abstract
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 (R) in streptavidin S112G and up to 80% ee (S) 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 Ka = 7.7 for avidin (pI = 10.4) and log Ka = 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.
Related Papers
- → Switchavidin: Reversible Biotin–Avidin–Biotin Bridges with High Affinity and Specificity(2014)36 cited
- → A comparison of the binding of biotin and biotinylated macromolecular ligands to an anti-biotin monoclonal antibody and to streptavidin(1993)25 cited
- → Methods to determine biotin-binding capacity of streptavidin-coated magnetic particles(1999)21 cited
- → Cellular Uptake of Fluorescent Labelled Biotin–Streptavidin Microspheres(2008)16 cited
- → Oligonucleotide-Blocked Streptavidin for Biotinylation Analysis(2022)2 cited