Role of NAD(P)H:quinone oxidoreductase encoded by drgA gene in reduction of exogenous quinones in cyanobacterium synechocystis sp. PCC 6803 cells

Biochemistry (Moscow)

Volumn 69, Issue 2, 2004, Pages 137-142

  Elanskaya, I V ^a   Grivennikova, V G ^a   Groshev, V V ^a   Kuznetsova, G V ^a   Semina, M E ^a   Timofeev, K N ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Cyanobacterium synechocystis sp. Pcc 6803; drgA gene; EPR spectroscopy; NAD(P)H:quinone oxidoreductase; P700+ reduction; Resistance to menadione

Indexed keywords

BACTERIA; BIOCHEMISTRY; CELL CULTURE; ELECTRON SPIN RESONANCE SPECTROSCOPY; GENES; GROWTH KINETICS; PHOTOOXIDATION; REDOX REACTIONS;

CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803 NAD(P)H; DRGA GENES; QUINONE OXIDOREDUCTASE; RESISTANCE TO MENADIONE;

ENZYMES;

BACTERIA (MICROORGANISMS); CYANOBACTERIA; INSERTION SEQUENCES; MAMMALIA; SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

BACTERIAL PROTEIN; CHLOROPHYLL; CHLOROPHYLL P700; MENADIONE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

ANTIBIOTIC RESISTANCE; ARTICLE; CYANOBACTERIUM; DRUG EFFECT; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PHOTOSYSTEM I;

BACTERIAL PROTEINS; CHLOROPHYLL; CYANOBACTERIA; DRUG RESISTANCE, BACTERIAL; MUTAGENESIS, INSERTIONAL; NAD(P)H DEHYDROGENASE (QUINONE); OXIDATION-REDUCTION; PHOTOSYSTEM I PROTEIN COMPLEX; QUINONES; VITAMIN K 3;

EID: 3543088741     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIRY.0000018943.21179.ba     Document Type: Article

References (36)

1. Hassan, H. M., and Fridovich, I. (1979) Arch. Biochem. Biophys., 196, 385-395.
2. Thor, H., Smith, M. T., Hartzell, P., Bellomo, G., Jewell, S., and Orrenius, S. (1982) J. Biol. Chem., 257, 12419-12425.
3. Lind, C., Hochstein, P., and Ernster, L. (1982) Arch. Biochem. Biophys., 216, 178-185.
4. Cenas, N., Anusevicius, Z., Bironaite, D., Bachmanova, G. I., Archakov, A. I., and Ollinger, K. (1994) Arch. Biochem. Biophys., 315, 400-406.
5. Pritsos, C. A., and Gustafson, D. L. (1994) Oncol. Res., 6, 477-481.
6. Tedeschi, G., Zetta, L., Negri, A., Mortano, M., Ceciliani, F., and Ronchi, S. (1997) Biochemistry, 36, 16221-16230.
7. Iyanagi, T., and Yamazaki, I. (1970) Biochim. Biophys. Acta, 216, 282-294.
8. Hauska, G. (1977) in Encyclopedia of Plant Physiology (Trebst, A., and Avron, M., eds,) Springer-Verlag, Berlin, Vol. 5, pp. 253-265.
9. Samuilov, V. D., Barskii, E. L., and Kitashov, A. V. (1997) Biochemistry (Moscow), 62, 909-913.
10. Samuilov, V. D., Borisov, A. Yu., Barsky, E. L., Borisova, O. F., and Kitashov, A. V. (1998) Biochem. Mol. Biol. Int., 46, 333-341.
11. Cooley, J. W., and Vermaas, W. F. J. (2001) J. Bacterial., 183, 4251-4258.
12. Howitt, C. A., Udall, P. K., and Vermaas, W. F. J. (1999) J. Bacteriol., 181, 3994-4003.
13. Hauska, G., Reimer, S., and Trebst, A. (1974) Biochim. Biophys. Acta, 357, 1-13.
14. Prochaska, H. J., De Long, M. J., and Talalay, P. (1985) Proc. Natl. Acad. Sci. USA, 82, 8232-8236.
15. Prochaska, H. J., and Talalay, P. (1986) J. Biol. Chem., 261, 1372-1378.
16. O'Brien, P. J. (1991) Chem. Biol. Interact., 80, 1-41.
17. Riley, R. J., and Workman, P. (1992) Biochem. Pharmacol., 43, 1657-1669.
18. Dinkova-Kostova, A. T., and Talalay, P. (2000) Free Rad. Biol. Med., 29, 231-240.
19. Ross, D., Kepa, J. K., Winski, S. L., Beall, H. D., Anwar, A., and Siegel, D. (2000) Chem. Biol. Interact., 129, 77-97.
20. Joseph, P., Long, D. J., 2nd, Klein-Szanto, A. J., and Jaiswal, A. K. (2000) Biochem. Pharmacol., 60, 207-214.
21. Radjendirane, V., Joseph, P., Lee, Y. H., Kimura, S., Klein-Szanto, A. J., Gonzalez, F. J., and Jaiswal, A. K. (1998) J. Biol. Chem., 273, 7382-7389.
22. Heflich, R. H., Howard, P. C., and Beland, F A. (1985) Mutat, Res., 149, 25-32.
23. Cresteil, T., and Jaiswal, A. K. (1991) Biochem. Pharmacol., 42, 1021-1027.
24. Trost, P., Bonora, P., Scagliarini, S., and Pupillo, P. (1995) Eur. J. Biochem., 234, 452-458.
25. Sparla, F., Tedesci, G., and Trost, P. (1996) Plant Physiol., 112, 249-258.
26. Sparla, F., Tedeshi, G., Pupillo, P., and Trost, P. (1999) FEBS Lett., 463, 382-386.
27. Matsuo, M., Endo, T., and Asada, K. (1998) Plant Cell Physiol., 39, 751-755.
28. Chesnavichene, E. A., Elanskaya, I. V., Bartsevich, V. V., and Shestakov, S. V. (1994) Dokl. Ross. Akad. Nauk, 334, 657-659.
29. Elanskaya, I. V., Chesnavichene, E. A., Vernotte, C., and Astier, C. (1998) FEBS Lett., 428, 188-192.
30. Rippka, R., Deruelles, J., Waterbury, J. B., Herdman, M., and Stanier, R. Y. (1979) J. Gen. Microbiol., 111, 1-61.
31. Mi, H., Endo, T., Ogawa, S., and Asada, K. (1995) Plant Cell Physlol., 36, 661-668.
32. Fulda, S., Huang, F., Nilsson, F., Hagemann, M., and Norling, B. (2000) Eur. J. Biochem., 267, 5900-5907.
33. Mi, H., Endo, T., Schreiber, U., Ogawa, S., and Asada, K. (1992) Plant Cell Physiol., 33, 1233-1237.
34. Cadenas, E., Boveris, A., Ragan, C. I., and Stoppani, A. O. (1977) Arch. Biochem. Biophys., 180, 248-257.
35. Imlay, J., and Fridovich, I. (1992) Arch. Biochem. Biophys., 296, 337-346.
36. Beyer, R. E., Segura-Aguilar, J., Di Bernardo, S., Cavazzoni, M., Fato, R., Fiorentini, D., Galli, M. C., Setti, M., Landi, L., and Lenaz, G. (1996) Proc. Natl. Acad. Sci. USA, 93, 2528-2530.