Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Effect of Herbicide Paraquat on NAD(H)-Redox-cycle

제초제 Paraquat의 NAD(H) 산화환원에 대한 영향

  • Kim Mi-Lim (Faculty of Cuisine & Nutrition, Daegu Haany University) ;
  • Choi Kyung-Ho (Department of Food Science and Nutrition, Daegu Catholic University)
  • 김미림 (대구한의대학교 식품조리영양학부) ;
  • 최경호 (대구가톨릭대학교 식품영양학과)
  • Published : 2005.04.01
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Abstract

This study was carried out to investigate the effect of herbicide paraquat (1,1-dimethyl-4,4-bipyridilium dichloride) on the electron transport system of the cell. When actively growing cells of bacteria were exposed to the 1.0 mM paraquat, more than $50\%$ of the cells were killed at 0 hour. But specific activities of superoxide dismutase (SOD) were not changed at 0 hour of paraquat treatment. Oxido-reductions of NAD (H) by the suspension of bacterial membtane, rat mithochondria and NAD-dependent dehydrogenase were accelerated by paraquat treatment.

생체세포에 대한 paraquat의 독작용은 superoxide dismutase 활성저해에 기인하는 것으로 알려져 있다. 그러나 세균이 paraquat에 매우 짧은 시간동안의 노출에 의하여서도 독작용을 받을 수 있는 것으로 검토됨에 따라 paraquat의 독작용의 하나로서 전자전달에 미치는 영향 중 NAD(H)의 산화 및 환원반응에 미치는 영향을 검토한 결과는 다음과 같다. 공시균의 원형질막 획분, rat mitocondria분산액 및 NAD-dependent dehydrogenase에 의한 산화 및 환원시 paraquat 첨가구에서 반응 Graph의 경사도가 더 컸으며, 반응 개시점 및 종결점이 대조구에 비해 낮은 결과로 반응이 가속화되는 결과를 볼 수 있었다. 반응을 경시적으로 NAD(H)의 함량변화로 검토한 결과에서도 원형질 막 획분과 rat mitocondria 분산액을 이용한 경우에 10분간의 NADH산화량이 대조구는 각각 960 mM, 1,187 mM이었으나 Paraquat 처리구는 각각 1,200 mM, 1,434 mM로 Paraquat 처리구가 반응 가속화 경향을 보였다. NAD(H) dependent dehydrogenase에 의한 NAD(H)의 산화 및 환원 반응에서도 대조구에 비하여 Paraquat 처리구가 초기반응의 가속화 및 총산화량의 증가를 보였다.

Keywords

References

  1. Agricultural chemical industrial association. 1995. pp182-187. Agrochemical year book
  2. Bader, J., Gunther, H., Nagata, S. and Simon, H. 1984. The reduction of NAD(P) by methylviologen cation radical catalyzed by different cells, mitochondria and enzymes. 'Conden:99992', Eur. Congr. Biotechnol. 3(1), 371-376
  3. Barceloux D. G. Ellenhorn M. J. 1991. Herbicides In. eds. Medical toxicology. pp1464-1468. 1st ed New York
  4. Bengis G. C. and Gromet E. Z. 1979. Purification of the energy transducingadenosin triphosphatase complex from Rhodospirillum rubrum. Biochem. 18, 3577-3581 https://doi.org/10.1021/bi00583a022
  5. Bullivant C. M. 1966. Accudental poisoning by paraquat. Report of 2 cases in man. Br. Med. J. 1, 1272-1273 https://doi.org/10.1136/bmj.1.5498.1272
  6. Chun, J. C., Lee, H. J. Ma, S. Y., and Kim, S. E. 1997. Physiological responses of Rhehmannia glutinosa to paraquat and its tolerance mechanism. Pestic. Biochem. Physiol. 59, 51-63
  7. Conning, D.M. and Fletcher, K. 1966. Paraquat and related bipyridyl. Br. Med. Bull. 25(3), 245-249
  8. Fuerst, E. P. and Norman, M. A. 1997. Interactions of cations with paraquat in leaf sections of resistant and sensitive biotypes of Conyza bonariensis. Pestic. Biochem. Physiol. 57, 181-191 https://doi.org/10.1006/pest.1997.2276
  9. Fuerst, E. P. and Vaughn, K. C. 1990. Mechanisms of paraquat resistance. Weed Technol. 4, 150-156
  10. Grupe, H. and Gottschalk, G. 1990. Clostricium acetobutylicum and the production of solvents, Gim 90 Conden: 9992 NO:PtII 715-729
  11. Gutmann, H. and Wahlfeld, A. W. 1985. Methods of enzymatic analysis. III. pp1464-1468. Academic Press Inc. New York and London
  12. Halliwell, B. 1978. Biochemical mechanisms accounting for toxic action of oxygen on living organisms : the sky role of superoxide dismutase. Cell Biol. Int. Rep. 2, 113-128 https://doi.org/10.1016/0309-1651(78)90032-2
  13. Harvey, B. M. R. and Harper, D. B. 1978. Mechanism of paraquat tolerance in pereniaI ryegrass: I .uptake, metabolism and translocation of paraquat. Plant Cell Environ. 1, 203-209 https://doi.org/10.1111/j.1365-3040.1978.tb00762.x
  14. Harvey, B. M. R. and Harper, D. B. 1978. Mechanism of paraquat tolerance in perenial ryegrass : II. role of superoxide dismutase, catalase and peroxidase. Plant Cell Environ. 1, 211-215 https://doi.org/10.1111/j.1365-3040.1978.tb00763.x
  15. Jang, E. J. 1987. Effect of paraquat on energy metabolism of Bacillus megaterium, 대구가톨릭대학교 석사학위논문
  16. Khan A. U. 1978. Activated oxygen singlet molecular oxygen and superoxide anion, Photochem. Photobiol. 28, 615-627 https://doi.org/10.1111/j.1751-1097.1978.tb06980.x
  17. Kim, C. S. and Choi, K. H. 1991. Effect of paraquat treatment on fatty acid composition of membrane lipids of Bacillus megaterium and Saccharomyces cerevisiae. Hyosung J. Appl. Sci. 53-61
  18. Kim, M. L. Park, C. S. and Choi, K. H. 1995. Inhibition of microbial growth by paraquat. Agri. Chem. Biotechnol. 38(4), 283-288
  19. Lebertz, H., White, H., Beer, A., Guther, H. and Simon, H. 1988. Enzyme activites clostridium thermoaceticum useful for preparative reductions carbon moonoxide as an electron donor. Dechema. Biotechnol. Conf. Coden :99992,5(5), 369-374
  20. Lee T. E., Park Y. H., Min Y. D.and Choi K. H. 2001. Inducibility of superoxide dismutase and metallothionein in the liver and kidney of mice by paraquatwith age. Korean J. Med. 61(4), 430-438
  21. Liochev, S. and Fridovich, I. 1986. Vanate-stimulated oxidation of NAD(P)H by biomembrane is a superoxid e-initiated radical chain reaction, Arch. Biochem. Biophy. 250, 139-145 https://doi.org/10.1016/0003-9861(86)90710-1
  22. Lowry, O. H., Rosebrough, N. J., Farr, A.L. and Randall, R. J. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem, 193, 265-275
  23. Maeda, H. and Kajiwara, S. 1985 Malic acid production by an electrochemical reduction system combined with the use of diaphorase and methylviologen. Biotechnol. Bioeng. 27(5), 596-602 https://doi.org/10.1002/bit.260270508
  24. Marklund, S. and Marklund, G. 1974. Involvement of the superoxide anion radical in the autoxidant of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47, 468-474
  25. Onyon L. J., Voalns G. N. 1987. The epidemiology and prevention of paraquat poisoning. Human Toxicol. 6, 19-29 https://doi.org/10.1177/096032718700600104
  26. Park K. I. 2003. Induction of iron superoxide dismutase by paraquat and iron in Vitreoscilla $C_1$. Korean J. Biotechnol. Bioeng. 18(6), 517-521
  27. Rao, G. and Mutharasan, R. 1985. Directed metabolic flow with high butanol yield and selectivity in continuous cultures of clostridium, Biotechnoi. Lett. 10(5), 313-318
  28. Simon, H., Bader, J., Guther, H., Neumann, S. and Thanos, J. 1984. Biohydrogenation and electromicrobial and electronenzymatic reduction method. 9, 171-185
  29. Singh, A. 1978. lnterconversion of singlet oxygen and related species. Photochem. Photobiol. 28, 429-433 https://doi.org/10.1111/j.1751-1097.1978.tb06942.x
  30. Wenning, P. J. and Richard T. D. 1988. The effects of paraquat microsomal oxygen reduction and antioxidant defemses in ribbed mussels and wedge clams, Mar. Environ. Res. 24, 301-305 https://doi.org/10.1016/0141-1136(88)90325-X
  31. Windholz, M. 1983. The merck Index & Co, 10th Edi. USA, No 6894