Abstract
© 2018 American Chemical Society. 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 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.
Original language | English |
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Pages (from-to) | 1476-1484 |
Number of pages | 9 |
Journal | ACS Catalysis |
Volume | 8 |
Issue number | 2 |
Early online date | 5 Jan 2018 |
DOIs | |
Publication status | Published - 2 Feb 2018 |
Keywords
- anionâï€ catalysis
- artificial metalloenzyme
- chimeric protein
- protein design
- protein engineering
- ring-closing metathesis
- transfer hydrogenation