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Published on: January 12, 2009
Design of peptide-containing N5-unmodified neutral flavins that catalyze aerobic oxygenations
Yukihiro Arakawa1, Ken Yamanomoto1, Hazuki Kita1
1Department of Applied Chemistry , Tokushima University , Minamijosanjima , Tokushima 770-8506 , Japan .
Abstract:
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, Fl , compared to those of FlEt , FlEt , and Fl-Enz, Fl. 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) 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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