Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesignElectronic supplementary information (ESI) available: All experimental procedures as well as synthesis and characterization of flavins 2–6, UV-vis of free and bound compound 3and NMR spectra are included. See DOI: 10.1039/c1cc14039f

By cofactor redesign, self-sufficient monooxygenases could be prepared. Tight binding of N-alkylated flavins to riboflavin-binding protein results in the creation of artificial flavoenzymes capable of H2O2-driven enantioselective sulfoxidations. By altering the flavin structure, opposite enantioselectivities could be achieved, in accordance with the binding mode predicted by in silicoflavin-protein docking of the unnatural flavin cofactors. The study shows that cofactor redesign is a viable approach to create artificial flavoenzymes with unprecedented activities. [ABSTRACT FROM AUTHOR]