Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein

Free Radical Biology and Medicine

Volumn 28, Issue 1, 2000, Pages 108-120

  Poole, Leslie B ^a   Higuchi, Masako ^b   Shimada, Mamoru ^c   Li Calzi, Marco ^a   Kamio, Yoshiyuki ^b  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b TOHOKU UNIVERSITY   (Japan)

^c Nippon Paint Co Ltd ^*  (Japan)

Author keywords

Alkyl hydroperoxide reductase; Disulfide reductase; Flavoprotein; Free radicals; NADH oxidase; Peroxidase; Peroxiredoxin; Redox centers

Indexed keywords

FLAVOPROTEIN; FREE RADICAL; OXIDOREDUCTASE; PEROXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; BACTERIAL PROTEIN; HYBRID PROTEIN; HYDROGEN PEROXIDE; NADPH OXIDASE 1; PEROXIREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENE SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; SALMONELLA TYPHIMURIUM; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STREPTOCOCCUS MUTANS; BACTERIAL GENE; CLASSIFICATION; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; SPECIES DIFFERENCE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; GENES, BACTERIAL; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; HYDROGEN PEROXIDE; MOLECULAR SEQUENCE DATA; NADH, NADPH OXIDOREDUCTASES; PEROXIDASES; RECOMBINANT FUSION PROTEINS; SALMONELLA TYPHIMURIUM; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STREPTOCOCCUS MUTANS;

EID: 0033621685     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00218-X     Document Type: Article

References (33)

1. Hamada S., Slade H.D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol. Rev. 44:1980;331-384.
2. Higuchi M. Effect of oxygen on the growth and mannitol metabolism of Streptococcus mutans. J. Gen. Microbiol. 130:1984;1819-1826.
3. Higuchi M. Reduced nicotinamide adenine dinucleotide oxidase involvement in defense against oxygen toxicity of Streptococcus mutans. Oral Microbiol. Immun. 7:1992;309-314.
4. 2O-forming oxidase induced in Streptococcus mutans. J. Gen. Microbiol. 139:1993;2343-2351.
5. 2-forming NADH oxidase from Streptococcus mutans. Biosci. Biotech. Biochem. 58:1994;1603-1607.
6. Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes . Proc. Natl. Acad. Sci. USA. 91:1994;7017-7021.
7. Poole L.B. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry. 35:1996;65-75.
8. Matsumoto J., Higuchi M., Shimada M., Yamamoto Y., Kamio Y. Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans. Biosci. Biotech. Biochem. 60:1996;39-43.
9. Ross R.P., Claiborne A. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. J. Mol. Biol. 227:1992;658-671.
10. Storz G., Jacobson F.S., Tartaglia L.A., Morgan R.W., Silveira L.A., Ames B.N. An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli genetic characterization and cloning of ahp . J Bacteriol. 171:1989;2049-2055.
11. Li Calzi M., Poole L.B. Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase. Biochemistry. 36:1997;13357-13364.
12. Poole L.B. The Salmonella typhimurium alkyl hydroperoxide reductase enzyme system. Stevenson K.J., Massey V., Williams C.H. Jr. Flavins and Flavoproteins 1996. 1997;751-760 University of Calgary Press, Calgary, Alberta, Canada.
13. Poole L.B., Shimada M., Higuchi M. NADH oxidase-1 and a second component encoded upstream of nox1 comprise an alkyl hydroperoxide reductase system in Streptococcus mutans. Stevenson K.J., Massey V., Williams C.H. Jr. Flavins and Flavoproteins 1996. 1997;769-772 University of Calgary Press, Calgary, Alberta, Canada.
14. Niimura Y., Poole L.B., Massey V. Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl hydroperoxide reductase flavoprotein component show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl hydroperoxide reductase 22-kDa protein component. J. Biol. Chem. 269:1995;25645-25650.
15. Niimura Y., Ohnishi K., Nishiyama Y., Kawasaki S., Miyaji T., Suzuki H., Nishino T., Massey V. Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein. Stevenson K.J., Massey V., Williams C.H. Jr. Flavins and Flavoproteins 1996. 1997;741-750 University of Calgary Press, Calgary, Alberta, Canada.
16. Koyama N., Koitabashi T., Niimura Y., Massey V. Peroxide reductase activity of NADH dehydrogenase of an alkaliphilic Bacillus in the presence of a 22-kDa protein component from Amphibacillus xylanus. Biochem. Biophys. Res. Commun. 247:1998;659-662.
17. Loprasert S., Atichartpongkun S., Whangsuk W., Mongkolsuk S. Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase gene and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX. J. Bacteriol. 179:1997;3944-3949.
18. Niimura Y., Massey V. Reaction mechanism of Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein. J. Biol. Chem. 271:1996;30459-30464.
19. Higuchi M., Yamamoto Y., Poole L.B., Shimada M., Sato Y., Takahashi N., Kamio Y. Functions for two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans. J. Bacteriol. 181:1999;5940-5947.
20. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Short protocols in molecular biology. 1992;John Wiley and Sons, New York.
21. Poole L.B., Ellis H.R. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry. 35:1996;56-64.
22. Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties. J. Biol. Chem. 264:1989;1488-1496.
23. Ellis H.R., Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry. 36:1997;13349-13356.
24. Shine J., Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature. 254:1975;34-38.
25. Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Ann. Rev. Gen. 13:1975;319-353.
26. Niimura Y., Ohnishi K., Yarita Y., Hidaka M., Masaki H., Uchimura T., Suzuki H., Kozaki M., Uozumi T. A flavoprotein functional as NADH oxidase from Amphibacillus xylanus Ep01 purification and characterization of the enzyme and structural analysis of its gene . J. Bacteriol. 175:1993;7945-7950.
27. Massey B., Palmer G. On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry. 5:1966;3181-3189.
28. Ellis H.R., Poole L.B. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry. 36:1997;15013-15018.
29. Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269:1994;27670-27678.
30. Poole L.B., Chae H.-Z., Flores B.M., Reed S.L., Rhee S.G., Torian B.E. Peroxidase activity of a TSA-like antioxidant protein from a pathogenic amoeba. Free Radic. Biol. Med. 23:1997;955-959.
31. Ohnishi K., Niimura Y., Yokoyama K., Hidaka M., Masaki H., Uchimura T., Suzuki H., Uozumi T., Kozaki M., Komagata K., Nishino T. Purification and analysis of a flavoprotein functional as NADH oxidase from Amphibacillus xylanus overexpressed in Escherichia coli. J. Biol. Chem. 269:1994;31418-31423.
32. Storz G., Christman M.F., Sies H., Ames B.N. Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. Proc. Natl. Acad. Sci. USA. 84:1987;8917-8921.
33. Greenberg J.T., Demple B. Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR- mutants. EMBO J. 7:1988;2611-2617.