Prof. Dr. Antonio Pierik
Structure, function and biosynthesis of iron-sulphur proteins
About one third of all proteins and half of all enzymes contain metal ions as cofactors. In most cases, the metal ions are the decisive component for the functionality of the biomolecules. Iron-sulphur proteins belong to one of the oldest and most interesting classes of metalloproteins. These contain inorganic clusters consisting of iron (Fe2+/Fe3+) and acid-labile sulphur (S2-) ions. The [2Fe-2S], [3Fe-4S] or [4Fe-4S] clusters are coordinated by heteroatoms in the side chains of the amino acids (usually cysteine).
Our research focuses on the functional analysis, bioinorganic chemistry, enzymology and biosynthesis of these Fe/S clusters. Bioinformatic, biochemical, genetic, electron paramagnetic resonance (EPR) and Mössbauer spectroscopic methods are used to discover, study and characterize new Fe/S proteins. Non-cysteine ligands are also identified. The group contributes to a better understanding of the function of biotechnologically important Fe/S dehydratases at the molecular level. In addition, we are developing new methods for more efficient cluster insertion by the cellular biosynthetic machinery.
Prof. Dr. Marcel Deponte
Comparative biochemistry
The Deponte group compares enzymes and protein complexes of the baker's yeast Saccharomyces cerevisiae and the parasites Leishmania tarentolae and Plasmodium falciparum. These unicellular organisms belong to three independent groups of eukaryotes and have a completely different way of life and biology. Thus, they are ideally suited for the identification of basic biochemical principles as well as parasite-specific properties.
We analyze enzyme mechanisms and protein structure-function relationships in detail. We use the following methods:
- Molecular modeling and other bioinformatic analyses as a basis for new hypotheses
- Steady-state and stopped-flow kinetic measurements with recombinant wild-type and mutant enzymes in vitro
- Heterologous complementation experiments, plasmid shuffling, CRISPR/Cas9 genetics and protein-protein interaction studies in S. cerevisiae, L. tarentolae and/or the human pathogenic malaria parasite P. falciparum