Bioanorganische Chemie (Ward)
Biocompatible Artificial Metalloenzymes
Merging organometallic chemistry with biotechnology
Artificial metalloenzymes
Organometallic- and enzymatic catalysis have evolved independently over the past four decades. In many respects, these approaches can be viewed as complementary. By incorporating an organometallic moiety within a protein host, we create artificial metallo-enzymes, with properties reminiscent both of homogeneous and enzymatic catalysis. The main focus of our research is to exploit such hybrid systems towards various applications.
- Enantioselective catalysis (white biotechnology)
- Synthetic biology (metabolic engineering)
- Bio-nanotechnology
In order to ensure unambiguous localisation of the organometallic moiety within the host protein, we rely on various anchoring strategies.
- Covalent anchoring exploiting carbonic anhydrase as scaffold
- Supramolecular anchoring exploiting the biotin-streptavidin couple
- Dative anchoring upon repurposing proteins with latent facial triad motifs
A Mosaic of applications
Reactions Implemented
- Hydrogenation
- Transfer hydrogenation
- Ketones, enones, imines, NAD(P)+
- Allylic substitution
- C-H activation
- Suzuki cross-coupling
- Metathesis
- Alcohol oxidation
- Sulfoxidation
- Dihydroxylation
- Peroxidation
- Michael addition
- Enzyme cascades
- DNA recognition
Current
- In vivo catalysis
- Directed evolution
- Alternative metabolism
- Cross-regulation
- Off-equilibrium thermodynamics
- Catalytic drugs
- Biofuels
- Multi-electron processes
- Artificial photosynthesis
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