Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes

Journal of Biological Chemistry

Volumn 282, Issue 2, 2007, Pages 929-937

  Jang, Soojin ^a   Imlay, James A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYL RADICALS; MICROBIAL GROWTH; MICROMOLAR CONCENTRATIONS;

AMINO ACIDS; BIOSYNTHESIS; ELECTRONS; ENZYMES; ESCHERICHIA COLI; IRON;

HYDROGEN PEROXIDE;

HYDROGEN PEROXIDE; IRON SULFUR PROTEIN; ISOMERASE; ISOPROPYLMALATE ISOMERASE; SCAVENGER; UNCLASSIFIED DRUG; CATALASE; ENZYME; ESCHERICHIA COLI PROTEIN; HYDROLYASE; HYDROXYL RADICAL; IRON; KATG PROTEIN, E COLI; OXALOACETATE TAUTOMERASE; OXIDIZING AGENT; PHOSPHOGLUCONATE DEHYDRATASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SULFUR;

ARTICLE; ENZYME INACTIVATION; ENZYME METABOLISM; ESCHERICHIA COLI; FENTON REACTION; IN VITRO STUDY; IN VIVO STUDY; INTRACELLULAR SPACE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FAMILY; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION;

ESCHERICHIA COLI; MAMMALIA;

CATALASE; ELECTRON TRANSPORT COMPLEX I; ENZYMES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDRO-LYASES; HYDROGEN PEROXIDE; HYDROXYL RADICAL; INTRAMOLECULAR OXIDOREDUCTASES; IRON; IRON-SULFUR PROTEINS; ISOMERASES; MUTATION; OXIDANTS; SULFUR;

EID: 33847753939     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M607646200     Document Type: Article

References (46)

1. Imlay, J. A. (2003) Annu. Rev. Microbiol. 57, 395-418
2. Seaver, L. C., and Imlay, J. A. (2001) J. Bacteriol. 183, 7182-7189
3. Griffiths, S. W., and Cooney, C. L. (2002) Biochemistry 41, 6245-6252
4. Winterbourn, C. C., and Metodiewa, D. (1999) Free Radic. Biol. Med. 27, 322-328
5. Halliwell, B., and Gutteridge, J. M. (1990) Methods Enzymol. 186, 1-85
6. Walling, C. (1975) Acc. Chem. Res. 8, 125-131
7. Rush, J. D., Maskos, Z., and Koppenol, W. H. (1990) FEBS Lett. 261, 121-123
8. Park, S., You, X., and Imlay, J. A. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 9317-9322
9. Aslund, F., Zheng, M., Beckwith, J., and Storz, G. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 6161-6165
10. Seaver, L. C., and Imlay, J. A. (2001) J. Bacteriol. 183, 7173-7181
11. Miller, J. H. (1972) Experiments in Molecular Genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
12. Datsenko, K. A., and Wanner, B. L. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 6640-6645
13. Kohlhaw, G. B. (1988) Methods Enzymol. 166, 423-429
14. Massey, V. (1955) Methods Enzymol. 1, 729-735
15. Gardner, P. R., and Fridovich, I. (1991) J. Biol. Chem. 266, 1478-1483
16. Matsushita, K., Ohnishi, T., and Kaback, H. R. (1987) Biochemistry 26, 7732-7737
17. Varghese, S. M., Tang, Y., and Imlay, J. A. (2003) J. Bacteriol. 185, 221-230
18. Wang, R. F., and Kushner, S. R. (1991) Gene (Amst.) 100, 195-199
19. Djaman, O., Outten, F. W., and Imlay, J. A. (2004) J. Biol. Chem. 279, 44590-44599
20. Flint, D. H., Emptage, M. H., and Guest, J. R. (1992) Biochemistry 31, 10331-10337
21. Mason, E. C., and Adarraga-Elizaran, A. (1963) J. Clin. Pathol. 16, 604-606
22. Hentze, M. W., and Argos, P. (1991) Nucleic Acids Res. 19, 1739-1740
23. Lauble, H., Kennedy, M. C., Beinert, H., and Stout, C. D. (1992) Biochemistry 31, 2735-2748
24. Gardner, P. R., and Fridovich, I. (1991) J. Biol. Chem. 266, 19328-19333
25. Kuo, C. F., Mashino, T., and Fridovich, I. (1987) J. Biol. Chem. 262, 4724-4727
26. Liochev, S. I., and Fridovich, I. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 5892-5896
27. Flint, D. H., Tuminello, J. F., and Emptage, M. H. (1993) J. Biol. Chem. 268, 22369-22376
28. Ohnishi, T. (1998) Biochim. Biophys. Acta 1364, 186-206
29. Flint, D. H. (1994) Arch. Biochem. Biophys. 311, 509-516
30. Brown, N. M., Kennedy, M. C., Antholine, W. E., Eisenstein, R. S., and Walden, W. E. (2002) J. Biol. Chem. 277, 7246-7254
31. Klebanoff, S. J., Locksley, R. M., Jong, E. C., and Rosen, H. (1983) CIBA Found. Symp. 99, 92-112
32. Wojtaszek, P. (1997) Biochem. J. 15, 681-692
33. Inbaraj, J. J., and Chignell, C. F. (2004) Chem. Res. Toxicol. 17, 55-62
34. Ran, H., Hassett, D. J., and Lau, G. W. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 14315-14320
35. Ito, A., Sato, Y., Kudo, S., Sato, S., Nakajima, H., and Toba, T. (2003) Curr. Microbiol. 47, 231-236
36. Pericone, C. D., Park, S., Imlay, J. A., and Weiser, J. N. (2003) J. Bacteriol. 185, 6815-6825
37. Lee, J. W., and Helmann, J. D. (2006) Nature 440, 363-367
38. Zheng, M., Wang, X., Templeton, L. J., Smulski, D. R., LaRossa, R. A., and Storz, G. (2001) J. Bacteriol. 183, 4562-4570
39. Touati, D., Jacques, M., Tardat, B., Bouchard, L., and Despied, S. (1995) J. Bacteriol. 177, 2305-2314
40. Liochev, S. I., and Fridovich, I. (1994) Free Radic. Biol. Med. 16, 29-33
41. Keyer, K., and Imlay, J. A. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 13635-13640
42. Almiron, M., Link, A. J., Furlong, D., and Kolter, R. (1992) Genes Dev. 6, 2646-2654
43. Altuvia, S., Almiron, M., Huisman, G., Kolter, R., and Storz, G. (1994) Mol. Microbiol. 13, 265-272
44. Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., and Chasteen, N. D. (2002) J. Biol. Chem. 277, 27689-27696
45. Neidhardt, F. C., Curtiss, R., III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E. (1996) in Escherichia coli and Salmonella (Neidhardt, F. C., ed) ASM Press, p. 2480, Washington, D. C.
46. Cherepanov, P. P., and Wackernagel, W. (1995) Gene (Amst.) 158, 9-14