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 feast is hardly understood.
We use protein crystallography in combination with protein chemistry and molecular biology to study molecular energy conversions.
Our 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 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