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Biophotonics encompass the interaction of biological systems with light. Here, light can either act as essential stimulus to regulate different biological processes, i.e. by the action of multi-domain photoreceptors, or is utilized to drive substrate conversion, i.e. by photocatalytic enzymes. Basic research within my group is focussed on flavin-binding blue-light photoreceptors of the light, oxygen, voltage (LOV) family and photocatalytic enzymes such as light-dependent protochlorophyllide oxidoreductases. We use molecular biological, microbiological, biochemical, as well spectroscopic methods to gain a broader understanding of the molecular principles underlying the function of those systems. In collaboration with different structural biology and biophysical research groups, we study structural aspects, conformational dynamics, and regulative protein-protein interactions.

From the understanding of basic structural and functional principles our work expands to biotechnological application. Projects include the use of flavin-binding LOV proteins as fluorescent reporters in biotechnological processes as well as engineering or design of artificial multi-domain proteins or regulatory systems (optogenetics). In more general terms, we engineer artificial multi-domain proteins for application in biotechnology, i.e. by recombining the functionality of different protein domains to yield novel functionalities. Here, for example novel enzyme immobilizates are generated by fusion of self-assembling protein domains or carrier-binding tags, which facilitate the easy and cost efficient production of sustainable enzyme immobilizates for application in synthetic chemistry and biocatalysis.


Molecular biological methods include rational protein design, site-directed and random mutagenesis and the construction of chimeric proteins by rational domain recombination. All design approaches are complemented by in vitro (and if possible in vivo) characterization by a variety of spectroscopic, biochemical and biophysical methods.

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