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Updated: Aug 12, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Substrate dehydrogenation by flavoproteins
1Department of Biochemistry and Biophysics and Department of Chemistry, Texas A&M University, College Station, TX 77843-2128, USA. fitzpat@tamu.edu
Abstract:
Enzymes with tightly bound FMN or FAD as cofactor catalyze the oxidation of a wide range of substrates. The chemical versatility of the isoalloxazine ring provides these enzymes with a range of potential mechanisms. Recent progress in elucidating the mechanisms of oxidation of organic substrates by flavoenzymes is described, focusing on the oxidation of alcohols, amino and hydroxy acids, amines, and nitroalkanes. With each family of enzymes, an attempt is made to integrate mechanistic, structural, and biomimetic data into a common catalytic mechanism.
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