Research interests of the AG Teufel

The Teufel laboratory provides an excellent opportunity for students who wish to explore microbial secondary metabolic pathways and exceptional enzymatic reactions that give rise to pharmaceutically relevant natural products or resistance to antibiotics.

Our studies currently focus on flavin-dependent enzymes that play pivotal roles in the generation of structurally complex natural product pharmacophores or their modification and thus inactivation. The importance of the flavin cofactor for countless redox reactions was recognized long ago, albeit mechanistic studies were heavily focused on a moderate assortment of primary metabolic flavoenzymes. While this granted deep insight into many aspects of flavin-dependent catalysis, the more recent detailed biochemical characterization of secondary metabolic pathways has proven a true treasure trove for flavin enzymology and unearthed a broader catalytic diversity.

It appears that the unmatched versatility of flavoenzymes is ideally suited for secondary metabolism, nature’s biosynthetic tinkering ground, and significantly contributes to the vast chemical and functional diversity of natural products such as antibiotics or anticancer agents.


Figure: Active site of the flavoenzyme EncM (left panel) that catalyzes an unprecedented oxidation reaction (right panel) during polyketide antibiotic biosynthesis.

For detailed information about our research program or to inquire about open positions, please contact PD Dr. Robin Teufel (E-mail: robin.teufel@zbsa.de).

Selected Publications

  • Frensch, B., Lechtenberg, T., Kather, M., Yunt, Z., Betschart, M., Kammerer, B., Lüdeke, S., Müller, M., Piel, J. & Teufel, R.* Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides. Nat. Commun., 12, 1431 (2021).
  • Duan Y., Petzold M., Saleem-Batcha R., Teufel R.* Bacterial tropone natural products and derivatives: Overview on the biosynthesis, bioactivities, ecological role and biotechnological potential. ChemBioChem, 21(17), 2384-407 (2020).
  • Matthews A., Saleem-Batcha R., Sanders JN., Stull F., Houk KN., & Teufel R.* Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases. Nat. Chem. Biol., 16(5), 556-63 (2020).
  • Tsypik O., Makitrynskyy R., Frensch B., Zechel DL., Paululat T., Teufel R.* (co-corresponding author), Bechthold A.* Oxidative carbon backbone rearrangement in rishirilide biosynthesis. J. Am. Chem. Soc. 142(13), 5913-17 (2020).
  • Saleem-Batcha R., Stull F., Sanders JN., Moore BS., Palfey BA., Houk KN.*, & Teufel R.* Enzymatic control of dioxygen binding and functionalization of the flavin cofactor. Proc. Natl. Acad. Sci. U S A. 115, 4909-14 (2018).
  • Teufel R., Kaysser L., Villaume MT., Diethelm S., Carbullido MK., Baran PS., & Moore BS.* One-pot enzymatic synthesis of merochlorin A and B. Angew. Chem. Int. Ed. 53, 11019-22 (2014).
  • Teufel R., Miyanaga A., Michaudel Q., Stull F., Louie G., Noel JP., Baran PS., Palfey B., & Moore BS.* Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature 503, 552-6 (2013).


  • DFG-Heisenberg Programme
  • DFG Research Grant “The Biosynthesis and Enzymology of Complex Rubromycin and Tropone Marine Bacterial Natural Products”
  • DFG Research Training Group 1976: “Functional Diversity of Cofactors in Enzymes
  • DFG-Emmy Noether Programme
  • Research Seed Capital – RiSC Ministry of Science, Research and the Arts of Baden-Württemberg (MWK)
  • „Innovationsfonds Forschung“ of the University Freiburg
  • DFG Postdoc Stipend



Center for Biological Systems Analysis

University of Freiburg


  • Address:

    Habsburgerstr. 49
    79104 Freiburg
  • Delivery entrance:

    Hauptstr. 1
    79104 Freiburg


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