Characterization in aqueous medium of an FMN semiquinone radical stabilized by the enzyme-like microenvironment of a modified polyethyleneimine.

The elusive flavin semiquinone intermediate found in flavoproteins such as cryptochromes has been obtained in aqueous solution by single electron reduction of the natural FMN cofactor using sodium ascorbate. This species was formed in the local hydrophobic microenvironment of a modified polyethyleneimine and characterized by UV-Visible, fluorescence and EPR spectroscopies.

Aerobic Baeyer-Villiger Oxidation Catalyzed by a Flavin-Containing Enzyme Mimic in Water.

Direct incorporation of molecular oxygen into small organic molecules has attracted much attention for the development of new environmentally friendly oxidation processes. In line with this approach, bioinspired systems mimicking enzyme activities are of particular interest since they may perform catalysis in aqueous media. Demonstrated herein is the incorporation of a natural flavin cofactor (FMN) into the specific microenvironment of a water-soluble polymer which allows the efficient reduction of the FMN by NADH in aqueous solution. Once reduced, this artificial flavoenzyme can then activate molecular dioxygen under aerobic conditions and result in the Baeyer-Villiger reaction at room temperature in water.