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Title

Characterization of a nitroreductase with selective nitroreduction properties in the food- and intestinal-occurring lactic acid bacterium Lactobacillus plantarum WCFS1

AuthorsGuillén, Hugo; Curiel, José Antonio ; Landete, José María ; Muñoz, Rosario ; Herraiz, Tomás
KeywordsNitroreductase
lactic acid bacteria
Lactobacillus plantarum fermentation
nitrobenzoate
nitrocompounds
quinone reductase
pyridinium cations
N-methyl-β-carbolines
Issue Date2009
PublisherAmerican Chemical Society
CitationJournal of Agricultural and Food Chemistry 57(21): 10457–10465 (2009)
AbstractNitroreductases reduce nitroaromatic compounds and other oxidants in living organisms, having interesting implications in environmental and human health. A putative nitrobenzoate reductase encoding gene (lp_0050) was recently annotated in the completed DNA sequence of lactic acid bacterium Lactobacillus plantarum WCFS1 strain. In this research, this L. plantarum gene was cloned and expressed, and the corresponding protein (PnbA) was biochemically characterized. This L. plantarum PnbA reductase is a 216 amino acid residue FMN-flavoprotein, which exhibits 23% identity with Pseudomonas putida and Ralstonia eutropha nitroreductases and <11% identity with those from enterobacteria such as E. cloacae. This reductase also showed 32-43% identity (65-72% similarity) to predicted PnbA proteins from other lactic acid bacteria. It utilized a wide range of electron acceptors including dichlorophenolindophenol (DCPIP), nitroblue tetrazolium (NBT), ferricyanide, and quinones (menadione, benzoquinone), but not pyridinium cations (paraquat and N-methyl-β-carbolines), and it was inhibited by dicoumarol and diphenyliodonium. HPLC-MS and spectroscopic data showed that it specifically catalyzed the reduction of the 4-nitroaromatic group to the corresponding hydroxylamine in the presence of NAD(P)H. Kinetics parameters (Vmax and Km) showed a higher efficiency for the reduction of 2,4-dinitrobenzoate than for the reduction of 4-nitrobenzoate. It was chemoselective for the reduction of 4-nitrobenzoates, being unable to reduce other nitroaromatics. Then, L. plantarum PnbA reductase might be more specific than other microbial nitroreductases that reduce a wider range of nitroaromatic compounds. The physiological and functional role of nitroreductases remain unknown; however, their presence in lactic acid bacteria widely occurring in foods and the human intestinal tract should be of further interest
Publisher version (URL)http://dx.doi.org/10.1021/jf9024135
URIhttp://hdl.handle.net/10261/47338
DOIhttp://dx.doi.org/10.1021/jf9024135
ISSN0021-8561
E-ISSN1520-5118
Appears in Collections:(IFI) Artículos
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