The Bischofs lab studies complex adaptive traits (CATs) of stressed bacteria. Our goals are to understand, to control and to engineer such traits. Using tools from molecular biology, microscopy and mathematical modelling we investigate how signaling networks regulate CATs. We seek to reveal fundamental organizing principles that relate the molecular network design to population-level behavior and vice versa. This should facilitate rational manipulations of bacterial populations and the implementation of novel functionalities into “smart” communities in the future.
Termite guts are tiny bioreactors converting lignocellulose to microbial fermentation products that fuel the metabolism of the host. My research group studies the role of the gut microbiota in the symbiotic digestion of wood, focusing on the structure and functions of the gut microbiome, the biology of the prokaryotic and eukaryotic symbionts and their interactions, and the evolution of the intestinal microbial community. Other aspects are the microbial processes in the guts of humivorous soil macrofauna, such as soil-feeding termites, scarab beetle larvae, and millipedes.
We use meta-omics approaches to understand the structural and functional responses of soil microbial communities to environmental change. In another line of research, we investigate the link between physiology and molecular biology of methanotrophic bacteria. Our model system is Methylocystis sp. strain SC2.
Methane is an end product of the anaerobic degradation of organic materials. This combustible gas is useful as a fuel but also it is a potential greenhouse gas. We are interested in the enzymes involved in methanogenesis from H2 and CO2. In the hydrogenotrophic methanogenic pathway, many unique enzymes are involved. These methanogenic enzymes contain novel cofactors and use unique coenzymes as the substrates. Our group examines the structure and function of the enzymes involved in hydrogenotrophic methanogenesis, the catalytic mechanism of [Fe]-hydrogenase, and the biosynthesis of the [Fe]-hydrogenase cofactor.