Research

Bioinorganic chemistry is a highly interdisciplinary branch of chemistry. We work together with people from different fields (biochemistry, chemical biology, microbiology, materials science, radiochemistry and spectroscopy) solving problems with a coordination chemist’s knowledge. The current team in the Daumann lab is an interdisciplinary mix from mainly synthetic chemists paired with biochemists and members that work on analytical techniques (EPR, NMR, HPLC-MS, GC-MS etc.).

Bioinorganic lanthanide and actinide chemistry

From technology applications in solar cells, mobile phones, batteries and lasers to counterfeiting tags in our Euro currency, lanthanides (Ln) have steadily made their way into our everyday lives. Together with Sc, Y and La, the lanthanides belong to the group of rare earth elements (REE). The term ‘rare’ is clearly misleading as many REEs are abundant, with Ce found in similar concentrations as Cu and Zn in the earth’s crust. What is currently lacking is an understanding and appreciation of the role of REEs in general, but especially the lanthanides (Ln), in biology. Remarkably, in 2014 it was discovered by H. Op den Camp, A. Pol and coworkers (A. Pol et al, Environ. Microbiol., 2014, 16, 255-264) that a methanotrophic microbe (SolV), isolated from volcanic mudpots near Naples, Italy, depends on lanthanides for growth. The respective enzyme responsible for this dependence is a methanol dehydrogenase (MDH). Our groups aims to gain a deeper understanding for lanthanides in living systems, using model complexes, kinetic studies of the enzymes themselves and various spectroscopic techniques to elucidate the mechanism of action of Ln-dependent MDH and other proteins.

Bioinorganic Iron Chemistry

Here we examine the key steps in the catalytic cycle of AlkBH- and TET-enzymes with the help of spectroscopic techniques and investigation of model complexes that mimic the function of these enzymes. Through a combined approach of rational design of model complexes paired with spectroscopic studies of the enzymatic systems, we hope to unravel the structure-reactivity relationships of TET/AlkBH-enzymes in epigenetic modifications ultimately resulting in a better understanding of the level of control by the catalytic domain in these transformations.