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Simulation of the monooxygenation function of flavoenzyme ( Fl-Enz ) has been long-studied with N 5-modified cationic flavins ( FlEt +  ), but never with N 5-unmodified neutral flavins ( Fl ) despite the fact that Fl is genuinely equal to the active center of Fl-Enz . This is because of the greater lability of 4a-hydroperoxy adduct of Fl , Fl OOH  , compared to those of FlEt +  , FlEt OOH  , and Fl-Enz , Fl OOH -Enz . In this study, Fl incorporated into a short peptide, flavopeptide ( Fl-Pep ), was designed by a rational top-down approach using a computational method, which could stabilize the corresponding 4a-hydroperoxy adduct ( Fl OOH -Pep ) through intramolecular hydrogen bonds. We report catalytic chemoselective sulfoxidation as well as Baeyer-Villiger oxidation by means of Fl-Pep under light-shielding and aerobic conditions, which are the first Fl-Enz -mimetic aerobic oxygenation reactions catalyzed by Fl under non-enzymatic conditions.

Design of peptide-containing N5-unmodified neutral flavins that catalyze aerobic oxygenations