Simulation of the monooxygenation function of flavoenzyme (>Fl-Enz) has been long-studied with N5-modified cationic flavins (>FlEt+), but never with N5-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, >FlOOH, compared to those of >FlEt+, >FlEtOOH, and >Fl-Enz, >FlOOH-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 (>FlOOH-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.
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