L
Livia Knörr
Researcher at University of Basel
Publications - 6
Citations - 1172
Livia Knörr is an academic researcher from University of Basel. The author has contributed to research in topics: Homogeneous catalysis & Streptavidin. The author has an hindex of 6, co-authored 6 publications receiving 1038 citations.
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Journal ArticleDOI
Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation
TL;DR: A bifunctional artificial metalloenzyme is created in which a glutamic acid or aspartic acid residue engineered into streptavidin acts in concert with a docked biotinylated rhodium(III) complex to enable catalytic asymmetric carbon-hydrogen (C–H) activation.
Journal ArticleDOI
Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes
Valentin Köhler,Yvonne M. Wilson,Marc Dürrenberger,Diego Ghislieri,Ekaterina Churakova,Tommaso Quinto,Livia Knörr,Daniel Häussinger,Frank Hollmann,Nicholas J. Turner,Thomas R. Ward +10 more
TL;DR: An artificial transfer hydrogenase, based on the incorporation of a biotinylated iridium-piano-stool complex in streptavidin, is shown to be fully compatible with a range of biocatalysts and enables the concurrent interplay with oxidative enzymes.
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Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines.
Marc Dürrenberger,Tillmann Heinisch,Yvonne M. Wilson,Thibaud Rossel,Elisa S. Nogueira,Livia Knörr,Annette Mutschler,Karoline Kersten,Malcolm Jeremy Zimbron,Julien Pierron,Tilman Schirmer,Thomas R. Ward +11 more
TL;DR: Introduction of a biotinylated iridium piano stool complex within streptavidin affords an artificial imine reductase (see scheme).
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OsO4·streptavidin: a tunable hybrid catalyst for the enantioselective cis-dihydroxylation of olefins.
Valentin Köhler,Jincheng Mao,Tillmann Heinisch,Anca Pordea,Alessia Sardo,Yvonne M. Wilson,Livia Knörr,Marc Creus,Jean-Christophe Prost,Tilman Schirmer,Thomas R. Ward +10 more
TL;DR: It is believed that both the OsO4- and NDO-catalyzed dihydroxylations proceed by an outer sphere [3+2] mechanism in which the substrate is not bound to the substrate, and the cissubstituted olefins are problematic.
Journal ArticleDOI
Genetic Optimization of the Catalytic Efficiency of Artificial Imine Reductases Based on Biotin–Streptavidin Technology
TL;DR: By introduction of lipophilic amino acid residues around the active site, an 8-fold increase in catalytic efficiency compared with the wild type imine reductase was achieved.