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. 1997 Sep;63(9):3691–3694. doi: 10.1128/aem.63.9.3691-3694.1997

Localization of the Enzyme System Involved in Anaerobic Reduction of Azo Dyes by Sphingomonas sp. Strain BN6 and Effect of Artificial Redox Mediators on the Rate of Azo Dye Reduction

M Kudlich, A Keck, J Klein, A Stolz
PMCID: PMC1389254  PMID: 16535698

Abstract

The effect of different artificial redox mediators on the anaerobic reduction of azo dyes by Sphingomonas sp. strain BN6 or activated sludge was investigated. Reduction rates were greatly enhanced in the presence of sulfonated anthraquinones. For strain BN6, the presence of both cytoplasmic and membrane-bound azo reductase activities was shown.

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Selected References

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  1. Adamson R. H., Dixon R. L., Francis F. L., Rall D. P. Comparative biochemistry of drug metabolism by azo and nitro reductase. Proc Natl Acad Sci U S A. 1965 Nov;54(5):1386–1391. doi: 10.1073/pnas.54.5.1386. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bironaite D. A., Cenas N. K., Kulys J. J. The rotenone-insensitive reduction of quinones and nitrocompounds by mitochondrial NADH:ubiquinone reductase. Biochim Biophys Acta. 1991 Oct 18;1060(2):203–209. doi: 10.1016/s0005-2728(09)91008-8. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  4. Brown J. P. Reduction of polymeric azo and nitro dyes by intestinal bacteria. Appl Environ Microbiol. 1981 May;41(5):1283–1286. doi: 10.1128/aem.41.5.1283-1286.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chung K. T., Stevens S. E., Jr, Cerniglia C. E. The reduction of azo dyes by the intestinal microflora. Crit Rev Microbiol. 1992;18(3):175–190. doi: 10.3109/10408419209114557. [DOI] [PubMed] [Google Scholar]
  6. Davies K. J., Doroshow J. H. Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase. J Biol Chem. 1986 Mar 5;261(7):3060–3067. [PubMed] [Google Scholar]
  7. Dubin P., Wright K. L. Reduction of azo food dyes in cultures of Proteus vulgaris. Xenobiotica. 1975 Sep;5(9):563–571. doi: 10.3109/00498257509056126. [DOI] [PubMed] [Google Scholar]
  8. Eggert C., Temp U., Dean J. F., Eriksson K. E. A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase. FEBS Lett. 1996 Aug 5;391(1-2):144–148. doi: 10.1016/0014-5793(96)00719-3. [DOI] [PubMed] [Google Scholar]
  9. Fujita S., Peisach J. The stimulation of microsomal azoreduction by flavins. Biochim Biophys Acta. 1982 Nov 24;719(2):178–189. doi: 10.1016/0304-4165(82)90087-3. [DOI] [PubMed] [Google Scholar]
  10. Gingell R., Walker R. Mechanisms of azo reduction by Streptococcus faecalis. II. The role of soluble flavins. Xenobiotica. 1971 May;1(3):231–239. doi: 10.3109/00498257109033172. [DOI] [PubMed] [Google Scholar]
  11. Gutman M., Singer T. P., Casida J. E. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XVII. Reaction sites of piericidin A and rotenone. J Biol Chem. 1970 Apr 25;245(8):1992–1997. [PubMed] [Google Scholar]
  12. Haug W., Schmidt A., Nörtemann B., Hempel D. C., Stolz A., Knackmuss H. J. Mineralization of the sulfonated azo dye Mordant Yellow 3 by a 6-aminonaphthalene-2-sulfonate-degrading bacterial consortium. Appl Environ Microbiol. 1991 Nov;57(11):3144–3149. doi: 10.1128/aem.57.11.3144-3149.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hernandez P. H., Gillette J. R., Mazel P. Studies on the mechanism of action of mammalian hepatic azoreductase. I. Azoreductase activity of reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Biochem Pharmacol. 1967 Oct;16(10):1859–1875. doi: 10.1016/0006-2952(67)90297-3. [DOI] [PubMed] [Google Scholar]
  14. Hernandez P. H., Mazel P., Gillette J. R. Studies on the mechanism of action of mammalian hepatic azoreductase. II. The effects of phenobarbital and 3-methylcholanthrene on carbon monoxide sensitive and insensitive azoreductase activities. Biochem Pharmacol. 1967 Oct;16(10):1877–1888. doi: 10.1016/0006-2952(67)90298-5. [DOI] [PubMed] [Google Scholar]
  15. Kawasaki S., Moriguchi R., Sekiya K., Nakai T., Ono E., Kume K., Kawahara K. The cell envelope structure of the lipopolysaccharide-lacking gram-negative bacterium Sphingomonas paucimobilis. J Bacteriol. 1994 Jan;176(2):284–290. doi: 10.1128/jb.176.2.284-290.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Keck A., Klein J., Kudlich M., Stolz A., Knackmuss H. J., Mattes R. Reduction of azo dyes by redox mediators originating in the naphthalenesulfonic acid degradation pathway of Sphingomonas sp. strain BN6. Appl Environ Microbiol. 1997 Sep;63(9):3684–3690. doi: 10.1128/aem.63.9.3684-3690.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kuhm A. E., Stolz A., Ngai K. L., Knackmuss H. J. Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J Bacteriol. 1991 Jun;173(12):3795–3802. doi: 10.1128/jb.173.12.3795-3802.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Leif H., Sled V. D., Ohnishi T., Weiss H., Friedrich T. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem. 1995 Jun 1;230(2):538–548. doi: 10.1111/j.1432-1033.1995.tb20594.x. [DOI] [PubMed] [Google Scholar]
  19. Majander A., Finel M., Wikström M. Diphenyleneiodonium inhibits reduction of iron-sulfur clusters in the mitochondrial NADH-ubiquinone oxidoreductase (Complex I). J Biol Chem. 1994 Aug 19;269(33):21037–21042. [PubMed] [Google Scholar]
  20. Nörtemann B., Baumgarten J., Rast H. G., Knackmuss H. J. Bacterial communities degrading amino- and hydroxynaphthalene-2-sulfonates. Appl Environ Microbiol. 1986 Nov;52(5):1195–1202. doi: 10.1128/aem.52.5.1195-1202.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Peterson F. J., Holtzman J. L., Crankshaw D., Mason R. P. Two sites of azo reduction in the monooxygenase system. Mol Pharmacol. 1988 Oct;34(4):597–603. [PubMed] [Google Scholar]
  22. Rafii F., Franklin W., Cerniglia C. E. Azoreductase activity of anaerobic bacteria isolated from human intestinal microflora. Appl Environ Microbiol. 1990 Jul;56(7):2146–2151. doi: 10.1128/aem.56.7.2146-2151.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Roxon J. J., Ryan A. J., Wright S. E. Enzymatic reduction of tartrazine by Proteus vulgaris from rats. Food Cosmet Toxicol. 1967 Nov;5(5):645–656. doi: 10.1016/s0015-6264(67)83216-4. [DOI] [PubMed] [Google Scholar]
  24. SCHMIDT K., LIAAENJENSEN S., SCHLEGEL H. G. DIE CAROTINOIDE DER THIORHODACEAE. I. OKENON ALS HAUPTEAROTINOID VON CHROMATIUM OKENII PERTY. Arch Mikrobiol. 1963 Aug 1;46:117–126. [PubMed] [Google Scholar]
  25. Scheline R. R., Nygaard R. T., Longberg B. Enzymatic reduction of the azo dye, acid yellow, by extracts of Streptococcus faecalis isolated from rat intestine. Food Cosmet Toxicol. 1970 Feb;8(1):55–58. doi: 10.1016/s0015-6264(70)80223-1. [DOI] [PubMed] [Google Scholar]
  26. Singer T. P., Ramsay R. R. The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase. Biochim Biophys Acta. 1994 Aug 30;1187(2):198–202. doi: 10.1016/0005-2728(94)90110-4. [DOI] [PubMed] [Google Scholar]
  27. Sutherland G. R., Khindaria A., Chung N., Aust S. D. The effect of manganese on the oxidation of chemicals by lignin peroxidase. Biochemistry. 1995 Oct 3;34(39):12624–12629. doi: 10.1021/bi00039a018. [DOI] [PubMed] [Google Scholar]
  28. Walker R. The metabolism of azo compounds: a review of the literature. Food Cosmet Toxicol. 1970 Dec;8(6):659–676. doi: 10.1016/s0015-6264(70)80455-2. [DOI] [PubMed] [Google Scholar]
  29. Weiss H., Friedrich T., Hofhaus G., Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur J Biochem. 1991 May 8;197(3):563–576. doi: 10.1111/j.1432-1033.1991.tb15945.x. [DOI] [PubMed] [Google Scholar]

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