|
|||||
|
|
NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role |
|
| Authors: | Sylvie Cortial Bogdan I Iorga Gilles Truan Philippe Meyer Jamal Ouazzani |
| Institution: | a Institut de Chimie des Substances Naturelles (ICSN), C.N.R.S. UPR 2301, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France b Laboratoire de chimie et biochimie des microorganismes, Université de Strasbour, 1 rue Blaise Pascal F-67070 Strasbourg, France c Microbiologie et Génétique Moléculaire, INRA (UMR1238) CNRS (UMR2585), AgroPariTech, F-78850 Thiverval-Grignon, France d Centre de Génétique Moléculaire (CGM), Avenue de la Terrasse, 91198 Gif-sur-Yvette cedex, France e Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France |
| Abstract: | 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 summaryMINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb:P39605) bind (MI:0407) by X-ray crystallography (MI:0114) |
| Keywords: | Nitroreductase NADH oxidase Hydrogen peroxide NAD+ degradation Crystal structure Bacillus subtilis |
| 本文献已被 ScienceDirect 等数据库收录！ | |