Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes
ACS Catal. 2018, 8, 1476-1484, 10.1021/acscatal.7b03773
The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric transfer hydrogenation, ring-closing metathesis and anion−π catalysis. The additional second coordination sphere elements significantly influence both the activity and the selectivity of the resulting hybrid catalysts. These findings lead to the identification of propitious chimeric streptavidins for future directed evolution efforts of artificial metalloenzymes.
Metal: IrReaction: Transfer hydrogenationMax TON: 970ee: 13PDB: ---Notes: ---
Metal: IrReaction: Transfer hydrogenationMax TON: 158ee: 82PDB: ---Notes: ---
Metal: RuLigand type: CarbeneReaction: Olefin metathesisMax TON: 105ee: ---PDB: ---Notes: RCM, biotinylated Hoveyda-Grubbs second generation catalyst
Metal: ---Ligand type: Biotinylated naphthalenediimidReaction: Anion-π catalysisMax TON: 6ee: 41PDB: ---Notes: No metal