Jörg Eppinger

Assistant Professor, Chemical Science
Physical Science and Engineering Division

Biological & Organometallic Catalysis Laboratories


Education Profile

  • Postdoctoral Fellow, The Scripps Research Institute, La Jolla, CA, U.S.A., 1999-2002
  • Dr. rer. nat., Technische Universität München, 1999
  • Dipl.-Chem., Technische Universität München, 1996

Research Interests

While commonly nature is considered a source of inspiration for chemists, organometallic and coordination chemistry provide a divers set of functions, which can be used to probe, augment and improve nature. Prof. Eppinger's research group combines homogeneous catalysis and synthetic biology to establish new catalysts for novel chemistry. Introducing tools and concepts of synthetic chemistry into living cells opens an unexplored research area, which integrates molecular catalysis' versatility and biocatalytic selectivity. Tailoring the interactions of molecular catalysts with biological ligands results in novel selectivities and reactivities. The four currently active research projects connect the interface of organometallic chemistry, molecular/microbiology and catalysis:
  • development of organometallic catalyst motifs, which are stable and active under physiological conditions. The design of catalysts motifs, which exhibit high activity at room temperature in water targets Green Chemistry applications and is a prerequisite for the synthesis of artificial metalloenzymes.
  • development tailored artificial metal centers in host-proteins. Integrating the specific advantages of organometallic catalysis and enzymes, these systems target in selective hydrogenations, cycloadditions, (amino)hydroxylations, C-H activation and cross–coupling reactions.
  • Discovery of novel organometallic mechanism in enzyme catalysis. This project targets to identify and characterize novel metalloproteins and to improve the knowledge about how a protein framework augments properties of metal centers. Characterization of iron sulfur cluster enzymes with organometallic intermediates and extremophilic Red Sea metalloenzymes are a current focus.
  • in vivo applications of metalloproteins and metal complexes. In an industry sponsored project we investigate artificial photosynthesis based on the combination of electrocatalytic CO2 reduction and microbial metabolism. Through collaborations, we have also reactivated biomedical projects and are currently exploring in vivo applications of the plethora of metal complexes available in our group. This includes cytotoxicity studies as well as the design of chemiluminescent metal complexes for cancer diagnostic.

Selected Publications

  • Grötzinger, S. W., Alam, I., Alawi, W. B., Bajic, V. B., Stingl, U., & Eppinger, J. (2015, July). Mining a database of single amplified genomes from Red Sea brine pool extremophiles—improving reliability of gene function prediction using a profile and pattern matching algorithm (PPMA). In The Proceedings from Halophiles 2013, the International Congress on Halophilic Microorganisms (p. 51). Frontiers Media SA.
  • Jantke, D., Marziale, A. N., Reiner, T., Kraus, F., Herdtweck, E., Raba, A., & Eppinger, J. (2013). Synthetic strategies for efficient conjugation of organometallic complexes with pendant protein reactive markers. Journal of Organometallic Chemistry, 744, 82-91.
  • Reiner, T., Jantke, D., Marziale, A. N., Raba, A., & Eppinger, J. (2013). Metal‐Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes. ChemistryOpen, 2(2), 50-54.
  • Mondal, M., & Bora, U. (2012). An efficient protocol for palladium-catalyzed ligand-free Suzuki–Miyaura coupling in water. Green Chemistry, 14(7), 1873-1876.
  • Gräwert, T., Span, I., Eisenreich, W., Rohdich, F., Eppinger, J., Bacher, A., & Groll, M. (2010). Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proceedings of the National Academy of Sciences, 107(3), 1077-1081.
  • Funeriu, D. P., Eppinger, J., Denizot, L., Miyake, M., & Miyake, J. (2005). Enzyme family–specific and activity-based screening of chemical libraries using enzyme microarrays. Nature biotechnology, 23(5), 622-627.