枯草芽孢杆菌中一种NADH：二氯靛酚氧化还原酶的特性研究
Characterization of a NADH:dichloroindophenol oxidoreductase from Bacillus subtilis.
作者信息
Nishiya Yoshiaki, Yamamoto Yoshihiro
机构信息
Tsuruga Institute of Biotechnology, Toyobo Co., Ltd, Tsuruga, Fukui, Japan.
出版信息
Biosci Biotechnol Biochem. 2007 Feb;71(2):611-4. doi: 10.1271/bbb.60548. Epub 2007 Feb 7.
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.
我们表达并纯化了一种来自枯草芽孢杆菌的偶氮还原酶同源物YvaB。发现YvaB具有NADH：2,6 - 二氯靛酚氧化还原酶活性以及偶氮还原酶活性。与大肠杆菌偶氮还原酶不同，纯化后的YvaB在没有黄素单核苷酸（FMN）的情况下仍具有活性。YvaB在pH 7.5和40摄氏度时活性最高，孵育30分钟后在高达55摄氏度的温度下仍保持稳定。值得注意的是，它在银离子（Ag(+)）存在的情况下保持稳定，并通过添加非离子洗涤剂而被激活。我们还研究了YvaB的其他酶学性质。
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