期刊
FEBS LETTERS
卷 584, 期 18, 页码 3916-3922出版社
WILEY
DOI: 10.1016/j.febslet.2010.08.019
关键词
Nitroreductase; NADH oxidase; Hydrogen peroxide; NAD(+) degradation; Crystal structure; Bacillus subtilis
NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H2O2 produced during the oxidative process or added exogenously. Structured summary: MINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb: P39605) bind (MI:0407) by X-ray crystallography (MI: 0114) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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