Related Experiment Video
Updated: Apr 5, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Flavin-dependent monooxygenases as versatile biocatalysts in biomanufacturing: mechanisms, engineering, and
Yong Li1,2, Ling Zhao1,2, Xin Pu1,2
1State Key Laboratory of Biopharmaceutical Preparation and Delivery, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, People's Republic of China.
Abstract:
Flavin-dependent monooxygenases (FMOs) are versatile oxidative biocatalysts that catalyze a wide array of oxygenation reactions, such as hydroxylation, epoxidation, Baeyer-Villiger oxidation, and halogenation. These enzymes utilize flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) as cofactors to mediate selective incorporation of oxygen into diverse substrates. Owing to their remarkable chemo-, regio-, and stereoselectivity, FMOs have attracted increasing attention as powerful tools for biomanufacturing. Recent advances in enzyme engineering, structural biology, and computational design have expanded the catalytic diversity of FMOs and enabled their integration into biocatalysis frameworks. Moreover, developments in cofactor regeneration, directed evolution, and cell-free biotransformation have improved FMOs' catalytic efficiency and scalability. Despite these advances, challenges such as limited thermostability, oxygen transfer efficiency, and substrate scope remain obstacles for industrial applications of FMOs. This review summarizes the structural characteristics, catalytic mechanisms, and engineering strategies of FMOs, highlights recent progress in their integration into biocatalysis platforms, and discusses current limitations and possible solutions. Insights into improving FMO catalytic performance and expanding their potential as next-generation biocatalysts for biosynthesis will be provided.
Related Concept Videos
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
Bioreactor Controls-III
Microbial Fermentation
Fates of Pyruvate
In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
Upstream Processing
Phase I Oxidative Reactions: Overview

