Chimeric streptavidins as host proteins for artificial metalloenzymes

Michela M. Pellizzoni, Fabian Schwizer, Christopher W. Wood, Valerio Sabatino, Yoann Cotelle, Stefan Matile, Derek N. Woolfson, Thomas R. Ward*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 languageEnglish
Pages (from-to)1476-1484
Number of pages9
JournalACS Catalysis
Issue number2
Publication statusPublished - 2 Feb 2018

Keywords / Materials (for Non-textual outputs)

  • anion π catalysis
  • artificial metalloenzyme
  • chimeric protein
  • protein design
  • protein engineering
  • ring-closing metathesis
  • transfer hydrogenation


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