Structural Biology and Biochemistry of Metalloenzymes

Research focus: Bacteria and Archaea have the ability to use carbon monoxide (CO), carbon dioxide (CO₂), and numerous pollutants as carbon and/or energy sources. In order 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 feast is hardly understood. 

We use protein crystallography in combination with protein chemistry and molecular biology to study molecular energy conversions.

Our short-term goals are to better understand 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.

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Current research area: How do enzymes help bacteria to convert C1 compounds?

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
10115 Berlin

Tel: ++49 30 2093 49840