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

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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, 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.

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

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Publication details

The article was received on 30 Apr 2017, accepted on 20 May 2017 and first published on 30 May 2017


Article type: Edge Article
DOI: 10.1039/C7SC01933E
Citation: Chem. Sci., 2017, Advance Article
  • Open access: Creative Commons BY license
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    Design of peptide-containing N5-unmodified neutral flavins that catalyze aerobic oxygenations

    Y. Arakawa, K. Yamanomoto, H. Kita, K. Minagawa, M. Tanaka, N. Haraguchi, S. Itsuno and Y. Imada, Chem. Sci., 2017, Advance Article , DOI: 10.1039/C7SC01933E

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