A5050764798- Peptidase Inhibition and Analysis
- Cyclopropane Reaction Mechanisms
- Click Chemistry and Applications
- Molecular Junctions and Nanostructures
- Enzyme Catalysis and Immobilization
- Biotin and Related Studies
- Advanced biosensing and bioanalysis techniques
- Chemical Synthesis and Analysis
- Signaling Pathways in Disease
- Biochemical and Structural Characterization
- Asymmetric Hydrogenation and Catalysis
- Catalytic C–H Functionalization Methods
- Photoreceptor and optogenetics research
- Metalloenzymes and iron-sulfur proteins
- CO2 Reduction Techniques and Catalysts
- Microbial Metabolism and Applications
- Radical Photochemical Reactions
University of Basel
2013-2021
Complementing enzymes in their native environment with either homogeneous or heterogeneous catalysts is challenging due to the sea of functionalities present within a cell. To supplement these efforts, artificial metalloenzymes are drawing attention as they combine attractive features both and enzymes. Herein we show that such hybrid consisting metal cofactor, cell-penetrating module, protein scaffold taken up into HEK-293T cells where catalyze uncaging hormone. This bioorthogonal reaction...
An artificial deallylase is constituted on the <italic>E. coli</italic> surface and genetically optimized for deprotection of caged aminocoumarin.
Artificial metalloenzymes enable the engineering of reaction microenvironment active metal catalyst by modification surrounding host protein. We report herein optimization an artificial imine reductase (ATHase) based on biotin–streptavidin technology. By introduction lipophilic amino acid residues around site, 8-fold increase in catalytic efficiency compared with wild type was achieved. Whereas substrate inhibition encountered for free cofactor and ATHase, two engineered systems exhibited...
Abstract Metal-catalyzed chemical transformations performed at the cellular level bear great potential for manipulation of biological processes. The complexity cell renders use transition metal chemistry difficult in systems. delivery reactive catalyst and control its spatial localization remain challenging. Here we report surface functionalization unicellular eukaryote Chlamydomonas reinhardtii with a tailor-made artificial metalloenzyme on-cell catalysis. functionalized cells viable are...
Abstract We report on the optimization of an artificial imine reductase based biotin‐streptavidin technology. With aim rapidly generating chemical diversity, a novel strategy for formation and evaluation biotinylated complexes is disclosed. Tethering biotin‐anchor to Cp* moiety leaves three free coordination sites d 6 metal introduction diversity by variety ligands. To test concept, 34 bidentate ligands were screened selection best was tested in presence 21 streptavidin (Sav) isoforms...
The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts artificial metalloenzymes (ArM) asymmetric transfer hydrogenation, ring-closing metathesis and anion−π catalysis. additional second coordination sphere elements significantly influence both the activity selectivity of resulting hybrid catalysts. findings lead to identification propitious streptavidins future directed evolution...
Artificial metalloenzymes (ArMs) combine characteristics of both homogeneous catalysts and enzymes. Merging abiotic biotic features allows for the implementation new-to-nature reactions in living organisms. Here, we present directed evolution an artificial metalloenzyme based on Escherichia coli surface-displayed streptavidin (SavSD hereafter). Through binding a ruthenium-pianostool cofactor to SavSD, allylic deallylase (ADAse hereafter) is assembled, which displays catalytic activity toward...
A dyad of covalently anchored [Ru(diimine)<sub>3</sub>]<sup>2+</sup> and a biotinylated triarylamine for the photogeneration charge-separated species within streptavidin.