Comparison of the azoreductase and nitroreductase from Clostridium perfringens

Author:

Rafii F1,Cerniglia C E1

Affiliation:

1. Division of Microbiology, National Center for Toxicological Research, Food and Drug Administration, Jefferson, Arkansas 72079.

Abstract

The purified azoreductase and nitroreductase of Clostridium perfringens, which have similar electrophoretic properties, both reacted in a Western blot (immunoblot) with a polyclonal antibody raised against the azoreductase. The activity of both enzymes was enhanced by flavin adenine dinucleotide and was inhibited by menadione, o-iodosobenzoic acid, and the antibody against azoreductase. Reduction of the azo dye Direct Blue 15 by the azoreductase was inhibited by nitroaromatic compounds. The apparent Km of the enzyme for reduction of Direct Blue 15 in the presence of 1-nitropyrene was higher than the Km with the azo dye alone, demonstrating competitive inhibition. The data show that the same protein is involved in the reduction of both azo dyes and nitroaromatic compounds.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference24 articles.

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2. Cerniglia C. E. 1985. Metabolism of 1-nitropyrene and 6-nitrobenzo[a]pyrene by intestinal microflora p. 133-137. In B. S. Wostmann (ed.) Germfree research: microflora control and its application to the biochemical sciences. Alan R. Liss New York.

3. Metabolism of azo dyes derived from benzidine, 3,3'- dimethylbenzidine and 3,3'-dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria;Cerniglia C. E.;Carcinogenesis,1982

4. Purification and characterization of a broad-specificity ,-glucosidase from sheep liver;Chinchetru M. A.;Int. J. Biochem.,1989

5. The metabolism of foreign compounds in the cestode, Moniezia expansa, and the nematode, Ascaris lumbncoides var. suum;Douch P. G. C.;Xenobiotica,1975

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