Center for Synthetic Microbiology
Karl-von-Frisch-Straße 8, 35042 Marburg
+49-6421 28 21527
We study anaerobic metabolic pathways for unusual substrates. Main interests are the molecular mechanisms and structure-function studies of metalloenzymes and the utilization of metabolic modules for designing novel synthetic pathways. A major focus of our research are the pathways of anaerobic hydrocarbon degradation.
In particular, we investigate the anaerobic degradation pathways of toluene, ethylbenzene, and indoleacetate. The former two are initiated by the glycyl-radical enzyme benzylsuccinate synthase and the molybdoenzyme ethylbenzene dehydrogenase, respectively. We also investigate the mechanisms of novel carboxylases for acetone, acetophenone and phenol, as well as the mechanism and maturation pathway of bacterial tungstoenzymes.
1. Arndt F, Schmitt G, Winiarska A, Saft M, Seubert A, Kahnt J, Heider J (2019) Characterisation of an aldehyde oxidoreductase from the mesophilic bacterium Aromatoleum aromaticum, a member of a new subfamily of tungsten-containing enzymes. Front Microbiol 10: 71..
2. Weidenweber S, Schühle K, Demmer U, Warkentin E, Ermler U & Heider J (2017) Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases. Nature Sci Rep 7: 39674.
3. Schühle K, Nies J & Heider J (2016) An indoleactate-CoA ligase and a phenylsuccinate CoA-transferase involved in anaerobic indoleacteate metabolism. Environ. Microbiol. 18: 3120-3132.