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NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological role.
- Source :
-
FEBS letters [FEBS Lett] 2010 Sep 24; Vol. 584 (18), pp. 3916-22. Date of Electronic Publication: 2010 Aug 18. - Publication Year :
- 2010
-
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 H(2)O(2) produced during the oxidative process or added exogenously.<br /> (Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Bacterial Proteins chemistry
Bacterial Proteins genetics
Cloning, Molecular
Molecular Sequence Data
Multienzyme Complexes chemistry
Multienzyme Complexes genetics
NAD metabolism
NADH, NADPH Oxidoreductases chemistry
NADH, NADPH Oxidoreductases genetics
Niacinamide biosynthesis
Nitroreductases chemistry
Nitroreductases genetics
Oxidative Stress
Protein Conformation
Superoxides metabolism
Bacillus subtilis enzymology
Bacterial Proteins physiology
Hydrogen Peroxide metabolism
Multienzyme Complexes physiology
NADH, NADPH Oxidoreductases physiology
Nitroreductases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 584
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 20727352
- Full Text :
- https://doi.org/10.1016/j.febslet.2010.08.019