Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes
| Autor: | Thomas R. Ward, Andreas Loosli, Julieta Gradinaru, Myriem Skander, Andrea Zocchi, Gérard Klein, Jerome Collot, Jerome Sauser, Nicolas Humbert, François Gilardoni |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Streptavidin Phosphines Stereochemistry Biotin chemistry.chemical_element Biochemistry Catalysis Enzyme catalysis Rhodium chemistry.chemical_compound Colloid and Surface Chemistry Metalloproteins biology Enantioselective synthesis Stereoisomerism General Chemistry Avidin Combinatorial chemistry Enzymes Kinetics Acrylates chemistry Stability constants of complexes Biotinylation Mutagenesis Site-Directed biology.protein Hydrogenation Bacillus subtilis |
| Zdroj: | Journal of the American Chemical Society. 126:14411-14418 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja0476718 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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