Research subject Enzyme catalysis

Nitrogen metabolism plays a central role in any organism. We are interested in more specifically identifying the difference in the pattern of proteins expressed when the bacterium fixes nitrogen compared with conditions when nitrogenase is not synthesized.

Enzymology is a cornerstone in the molecular life sciences. Rates of chemical reactions in cells and cellular signaling are governed by enzymes. It is becoming increasingly evident that enzymes are integral components of more wide-ranging molecular interactions such that the study of enzyme functions should be extended to their cellular context.

The enzyme ribonucleotide reductase (RNR) catalyses the reaction that provides new DNA building blocks. RNR is therefore a prerequisite in all living cells, and also regulates cellular replication and proliferation. Some antiproliferative drugs (e.g. hydroxyurea and gemcitabine) that are used clinically today are specific inhibitors of RNR.

Our main area of interest and expertise is how protein structure relates to function, in particular in proteins that utilize redox active metal cofactors or radicals for catalysis.

The botulinum neurotoxins are the most toxic substances known. Despite this, their therapeutic properties are becoming increasingly evident. We study these toxins using a variety of methods, including X-ray crystallography, to understand their mechanism of action, thereby enabling the development of their therapeutic properties. 

We use time-resolved spectroscopic techniques to study each component of the respiratory chain of aerobic bacteria - assemblies of components and intact mitochondrial membranes. A long-term goal is to visualize the dynamic processes of respiration in 3D - to reconstruct “molecular movies” showing functional dynamics of complex molecular machines in action.