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Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

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journal contribution
posted on 05.01.2018 by Michela M. Pellizzoni, Fabian Schwizer, Christopher W. Wood, Valerio Sabatino, Yoann Cotelle, Stefan Matile, Derek N. Woolfson, Thomas R. Ward
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.

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