Max Planck Fellows
Biogenesis of Iron–Sulfur Proteins in Eukaryotes and the Link to Cellular Iron Homeostasis
Iron-sulfur (Fe/S) clusters are ubiquitous and versatile protein cofactors used for catalysis, electron transfer, and sensing. In a living cell, these simple inorganic cofactors are synthesized and inserted into apoproteins by a surprisingly complex proteinaceous machinery involving the ISC assembly and export machineries of mitochondria, and the CIA machinery of the cytosol. The group of Prof. Dr. Roland Lill is interested in understanding the molecular mechanisms of Fe/S protein maturation. Yeast and human cell cultures are used as model systems. Since the efficiency of Fe/S protein maturation is intimately linked to cellular iron uptake and homeostasis, the group is trying to understand both the mechanisms of iron uptake regulation and the molecular basis that connects the two processes.
Mechanism of Enzymes from Anaerobic Bacteria (Prof. W. Buckel)
The group of Prof. Dr. Wolfgang Buckel focuses on the mechanisms of enzymes from anaerobic bacteria. The absence of oxygen enables anaerobes to use radical enzymes. The radicals are generated either by complex cofactors such as coenzyme B12 or by just transient one-electron oxidation or reduction. In all cases the radical or the electronis recycled after each turnover. Such enzymes that stabilize radical intermediates open a new chapter of chemical biology. Recently, enzymes were discovered that catalyze electron bifurcations, in which an exergonic reduction drives an endergonic reduction. This new reaction explains the long-time elusive energy metabolism of strict anaerobes, especially those of fermentative bacteria and cytochrome-less methanogens.