HIPS-Talk: "The biochemistry of vitamin B2 – a fresh look at an old cofactor"
The ubiquitous riboflavin (vitamin B2)-derived enzyme cofactors were discovered more than 80 years ago and soon shown to facilitate a multitude of essential enzymatic redox reactions in primary metabolism. More recently, it became evident that flavin-dependent enzymes also adopt an outstanding role in the generation of chemically complex natural products. Surprisingly, we discovered that one of these enzymes employs an unprecedented flavin-N5-oxide oxygenating species that is key to the formation of a structurally unique polyketide antibiotic in marine bacteria1,2. Our current efforts aim to elucidate the biological role, chemical properties, and enzymatic formation of this novel flavin redox state and it appears that there is still much to learn about the biochemistry of Vitamin B2.
1) 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).
2) Teufel R., Stull F., Meehan MJ., Michaudel Q., Dorrestein PC., Palfey BA., Moore BS. Biochemical establishment and characterization of EncM's flavin-N5-oxide cofactor. J Am Chem Soc 137, 8078-8085 (2015).
Building and room
Blg E8.1, Conference Room (Ground floor)
Dr. Robin Teufel
University of Freiburg
Prof. Dr. Rolf Müller