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Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

Pellizzoni, Michela M.
Schwizer, Fabian
Wood, Christopher W.
Sabatino, Valerio
Woolfson, Derek N.
Ward, Thomas R.
Published in ACS Catalysis. 2018, vol. 8, no. 1, p. 1476-1484
Abstract 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.
Keywords Anion−π catalysisArtificial metalloenzymeChimeric proteinProtein designProtein engineeringRing-closing metathesisTransfer hydrogenation
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Research group Groupe Matile
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PELLIZZONI, Michela M. et al. Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes. In: ACS Catalysis, 2018, vol. 8, n° 1, p. 1476-1484. doi: 10.1021/acscatal.7b03773 https://archive-ouverte.unige.ch/unige:101713

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Deposited on : 2018-01-29

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