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ID 115059
Author
Yamanomoto, Ken Tokushima University
Kita, Hazuki Tokushima University
Tanaka, Masami Tokushima Bunri University
Haraguchi, Naoki Toyohashi University of Technology
Itsuno, Shinichi Toyohashi University of Technology
Content Type
Journal Article
Description
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.
Journal Title
Chemical Science
ISSN
20416539
Publisher
The Royal Society of Chemistry
Volume
8
Issue
8
Start Page
5468
End Page
5475
Published Date
2017-05-30
Rights
This article is licensed under a Creative Commons Attribution 3.0 Unported Licence(https://creativecommons.org/licenses/by/3.0/).
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language
eng
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departments
Science and Technology
Liberal Arts and Sciences