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Updated: Jul 17, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
Characterization of a NADH:dichloroindophenol oxidoreductase from Bacillus subtilis
Yoshiaki Nishiya1, Yoshihiro Yamamoto
1Tsuruga Institute of Biotechnology, Toyobo Co., Ltd, Tsuruga, Fukui, Japan. yoshiaki_nishiya@bio.toyobo.co.jp
Abstract:
We expressed and purified an azoreductase homolog, YvaB, from Bacillus subtilis. YvaB was found to have NADH:2,6-dichloroindophenol oxidoreductase activity, as well as azoreductase activity. Purified YvaB was active without FMN, unlike Escherichia coli azoreductase. YvaB was most active at pH 7.5 and 40 degrees C, and was stable up to 55 degrees C after incubation for 30 min. Remarkably, it was stable in the presence of Ag(+), and was activated by the addition of non-ionic detergents. Other enzymatic properties of YvaB were also investigated.
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