Design and Realization of New CO₂- and C1-Converting Enzymes and pathways

Nature provides an incredible potential of enzymes for sustainable biocatalysis. To build new options in carbon capture, we leverage the natural versatility of enzymes to engineer and apply their activity towards converting one-carbon substrates like CO₂ and formate. This is achieved by employing targeted and untargeted enzyme engineering strategies, focusing on optimizing both reaction rate and substrate specificity. Our current efforts focus on:

• Enzymatic conversion of one-carbon substrates substrates (like CO₂ and formate) to value-added products
• Engineering “missing-link” enzymes that enable entirely new-to-nature pathways and alleviate bottlenecks in existing pathways
• Realizing new-to-nature pathways by combining enzymes from diverse organisms

Our institute provides a unique platform for accelerating enzyme discovery. We utilize a high-throughput screening system equipped with a robotics platform (MaxGENESYS) and a dedicated metabolomics core facility. This semi-automated setup allows for rapid evaluation of even intricate enzyme assays. Additionally, our interdisciplinary approach fosters collaboration between biochemists and strain engineers. By incorporating growth-coupled selection alongside traditional screening methods, we have successfully engineered "missing-link" enzymes that pave the way towards the establishment of entirely new metabolic pathways, while eliminating bottlenecks in existing ones (Scheffen et al. Nat Catal; Nattermann et al. Nat Comm).

Aligned with Max Planck's philosophy of "understanding preceding application", we prioritize fundamental research into enzyme structure and function. We have access to advanced biophysical techniques like X-ray crystallography, cryogenic electron microscopy, and deuterium exchange mass spectrometry to elucidate enzyme structure-function relationships (Stoffel et al. PNAS; Bernhardsgrütter et al. Nat Chem Biol).

To attain deeper insight into the evolutionary history and functional diversification of enzymes, we employ bioinformatic tools to help us understand the pathways of natural evolution (Schulz et al. Science). This enables us to understand enzymatic bottlenecks and find potential pathways to circumvent these. Beyond single enzymes, we also investigate higher order assemblies of enzymes and their function on catalysis, such as bacterial microcompartments and proteinaceous liquid-liquid phase separated condensates (Bernhardsgrütter et al. Nat Chem Biol).

 

Learn more about:
Evolution and Biochemistry of natural CO₂-fixing enzymes
in vitro synthetic metabolic networks
Transplantation of new CO₂-metabolism into natural cells
Phototrophic chassis
Design and realization of artificial organelles and cells

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