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Updated: Mar 18, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Characterization of iron-sulfur clusters in flavin-containing opine dehydrogenase
Seiya Watanabe1,2, Kunihiko Tajima3, Kazuma Matsui3
1a Department of Bioscience , Graduate School of Agriculture, Ehime University , Matsuyama , Japan.
Abstract:
Flavin-containing opine dehydrogenase from Bradyrhizobium japonicum forms a heterooligomeric α4β4γ4 enzyme complex. An electron paramagnetic resonance spectroscopy analysis using wild-type and site-directed mutants revealed that [4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the γ- and α-subunits, respectively. The latter was found to be important for structural folding and enzyme catalysis.
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