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Updated: Dec 17, 2025

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Flavin Nitroalkane Oxidase Mimics Compatibility with NOx/TEMPO Catalysis: Aerobic Oxidization of Alcohols, Diols, and
Pawan Thapa1, Shan Hazoor1, Bikash Chouhan1
1Department of Chemistry and Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019-0065, United States.
Abstract:
Biomimetic flavin organocatalysts oxidize nitromethane to formaldehyde and NO-providing a relatively nontoxic, noncaustic, and inexpensive source for catalytic NO2 for aerobic TEMPO oxidations of alcohols, diols, and ethers. Alcohols were oxidized to aldehydes or ketones, cyclic ethers to esters, and terminal diols to lactones. In situ trapping of NO and formaldehyde suggest an oxidative Nef process reminiscent of flavoprotein nitroalkane oxidase reactivity, which is achieved by relatively stable 1,10-bridged flavins. The metal-free flavin/NOx/TEMPO catalytic cycles are uniquely compatible, especially compared to other Nef and NOx-generating processes, and reveal selectivity over flavin-catalyzed sulfoxide formation. Aliphatic ethers were oxidized by this method, as demonstrated by the conversion of (-)-ambroxide to (+)-sclareolide.
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