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

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_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</

SUBMITTER: Arakawa Y 

PROVIDER: S-EPMC6102831 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature