Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 28, Issue 7, Pages 1132-1136Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0891-5849(00)00208-2
Keywords
protein nitration; peroxynitrite; nitrofurantoin; aminotyrosine; free radicals
Funding
- NHLBI NIH HHS [HL 54926] Funding Source: Medline
- NIA NIH HHS [AG 13966] Funding Source: Medline
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The oxygen-insensitive nitroreductases nfsA and nfsB are known to reduce para-nitrated aromatic com pounds. We tested the hypothesis that these nitroreductases are capable of reducing S-nitrotyrosine in proteins and peptides, as well as in free amino acids using wild-type and nfsA nfsB mutant strains of Escherichia coli. E. coli homogenates were incubated with nitrated proteins and the level of S-nitrotyrosine immunoreactivity was assayed by Western blotting. Assay conditions that allow the nitroreductases to rapidly reduce nitrofurantoin did not result in the modification of 3-nitrotyrosine in protein, peptide, or free amino acid. Stimulation of nfsA nfsB activity with paraquat had no effect on 3-nitrotyrosine reduction. Nonlethal exposure of E. roll to peroxynitrite/CO2 resulted in the reproducible nitration of tyrosine residues in endogenous proteins. The degree of 9-nitrotyrosine immunoreactivity over the 2-h postexposure period did not differ between mutant and wild-type strains. These results indicate that the nfsA and nfsB enzymes do not reduce 3-nitrotyrosine. (C) 2000 Elsevier Science Inc.
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