Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 349, Issue 11-12, Pages 1923-1930Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.200700022
Keywords
artificial metalloenzymes; biotin-avidin; chemogenetic optimization; enantioselective catalysis; enzyme immobilization; hydrogenation
Categories
Ask authors/readers for more resources
We report on our efforts to create efficient artificial metalloenzymes for the enantioselective hydrogenation of N-protected dehydroamino acids using either avidin or streptavidin as host proteins. Introduction of chiral amino acid spacers-phenylalanine or proline - between the biotin anchor and the flexible aminodiphosphine moiety 1, combined with saturation mutagenesis at position S112X of streptavidin, affords second generation artificial hydrogenases displaying improved organic solvent tolerance, reaction rates (3-fold) and (S)-selectivities (up to 95% ee for N-acetamidoalanine and N-acetamidophenylalanine). It is shown that these artificial with an increased affinity for the substrate and a higher k(cat) than the protein-free catalyst (compare(cat) 3.06 min(-1) and K-M 7.38 mNl for [Rh(COD)Biot-1](+) with k(cat) 12.30 min(-1) and K-M 4.36 mM for [Rh(COD)Biot-(R)-Pro-1](+) subset of WT Sav). Finally, we present a straightforward protocol using Biotin-Sepharose to immobilize artificial metalloenzymes (> 92 % ee for N-acetamidoalanine and N-acetamidophenylalanine using [Rh(COD)Biot-(R)-Pro-1](+) subset of Sav S112W).
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available