Structural Biology and Biochemistry of Metalloenzymes
Research focus: Bacteria and Archaea can use carbon monoxide (CO), carbon dioxide (CO2), and numerous pollutants as carbon and/or energy sources. To activate and convert these inert compounds, the organisms use complex metalloenzymes that catalyze reactions under mild cellular conditions. For comparison, in a chemistry laboratory, similar reactions are only possible with valuable catalysts under high pressure and temperatures. How these metal-containing enzymes achieve this feat is hardly understood.
We use protein crystallography in combination with protein chemistry and molecular biology to investigate molecular energy conversions.
Our goals are to gain a deeper understanding of the molecular basis of catalytic processes and the evolution of enzymes. Our long-term goal is to evolve new (bio)catalysts for the energy-efficient use of CO2 and CO, as well as for the (bio)degradation of pollutants.
Keep up with the latest news on Bluesky (@dobbek-lab.bsky.social) and Twitter (@Dobbek_SBBC_Lab)
Current research areas:
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C1 metabolism: Carbon monoxide dehydrogenases (CODH), acetyl-CoA synthase (ACS), Corrinoid Iron-Sulfur protein (CoFeSP), and auxiliary enzymes/proteins
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Double-cubane cluster proteins and ATP-dependent reductions (DCCP/DCCP-R systems) (work in progress)
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Artificial enzymes for new reactivities (Sulerythrin and hexameric tyrosine-coordinated heme proteins, HTHP) (work in progress)
Previous projects:
How are aromatic compounds degraded?
How do enzymes generate radical intermediates?
Humboldt-Universität zu Berlin
Lebenswissenschaftliche Fakultät, Institut für Biologie
Strukturbiologie/Biochemie
Prof. Dr. Holger Dobbek
Philippstr. 13, Leonor Michaelis Haus (Haus 18)
10115 Berlin
Tel: +49 30 2093 49840