Biological roles of rare earth elements
From technology applications in solar cells, mobile phones, batteries and lasers to counterfeiting tags in our Euro currency, Rare Earth Elements (REEs) have steadily made their way into our everyday lives. 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 those systems. We are using model complexes and various spectroscopic techniques to elucidate the mechanism of action of this REE-dependent MDH.
Bioinspired degradation of endocrine disrupting chemicals (EDC)
Human and industrial waste management and the widespread use of pesticides have contributed to the accumulation of endocrine disrupting chemicals (EDC, e.g. DDT, BPA) in the environment. Due to the widespread use of EDC some organisms have evolved enzymes that are capable of degrading those chemicals (e.g. DDT Dehydrochlorinase). Other natural enzymes such as laccase, cytochrome P450 or manganese peroxidase enzymes have been shown to be able to degrade certain EDCs. We are interested in developing bio-inspired methods for water purification filter systems.
Mechanistic studies of TET-enzyme model complexes for the elucidation of epigenetically relevant demethylation mechanisms
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.