Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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The Membrane-Bound NADH:Ubiquinone Oxidoreductase in the Aerobic Respiratory Chain of Marine Bacterium Pseudomonas nautica

  • Lee, Young-Jae (Department of Microbiology, College of Natural Sciences, Changwon National University) ;
  • Cho, Kyeung-Hee (Department of Microbiology, College of Natural Sciences, Changwon National University) ;
  • Kim, Young-Jae (Department of Microbiology, College of Natural Sciences, Changwon National University)
  • Published : 2003.04.01
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Abstract

Each oxidoreductase activity of the aerobic respiratory chain-linked NADH oxidase system in the marine bacterium Pseudomonas nautica was stimulated by monovalent cations including $Na^+,\;Li^+,\;and\;K^+$. In the presence of NADH or deamino-NADH as electron donors, $GH_2$ formation was approximately 1.3-fold higher in the presense of 0.08 M of $Na^+\;than\;K^+$, Whereas the other reductase activities were not significantly higher in $Na^+\;than\;K^+$. The optimal pH of NADH (or deamino-NADH):ubiquinone-1 oxidoreductase was 9.0 in the presence of 0.08 M NaCl. The activity of NADH (or deamino-NADH):ubiquinone-1 oxidoreductase was inhibited by about 33% with $60{\mu}M$ 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO). The activity of NADH (deamino-NADH): ubiquinone-1 oxidoreductase was inhibited by about 32 to 38% with $80{\mu}M$ rotenone, whereas the activity was highly resistant to capsaicin. On the other hand, electron transfer from NADH or deamino-NADH to ubiquinone-1 generated a membrane potential (${\Delta}{\psi}$) which was larger in the presence of $Na^+$ than that observed in the absence of $Na^+$. The ${\Delta}{\psi}$ was almost completely collapsed by $5{\mu}M$ carbonylcyanide m-chlorophenylhydrazone(CCCP), and approximately 50% inhibited by $100{\mu}M$ rotenone, or $60{\mu}M$ 2-heptyl-4-hydroxyquinoline (HQNO). Also, HQNO made the ${\Delta}{\psi}$ very unstable. The results suggest that the enzymatic and energetic properties of the NADH:ubiquinone oxidoreductase of P. nautica are quite different, compared with those of other marine halophilic bacteria.

Keywords

References

  1. Mol. Cells v.10 Enzymatic and energetic properties of the aerobic respiratory chain-linked NADH oxidase system in the marine bacterium Pseudomonas nautica Cho, K. H.;Y. J. Kim
  2. FEBS Lett. v.122 A new sodium transport system energized by the decarboxylation of oxaloacetate Dimroth, P. https://doi.org/10.1016/0014-5793(80)80446-7
  3. Eur. J. Biochem. v.115 Characterization of a membrane-bound biotin enzyme: Oxaloacetate decarboxylase from Klebsiella aerogenes Dimroth, P. https://doi.org/10.1111/j.1432-1033.1981.tb05245.x
  4. Ann. N. Y. Acad. Sci. v.447 Biotin-dependent decarboxylases as energy transducing systems Dimroth, P https://doi.org/10.1111/j.1749-6632.1985.tb18426.x
  5. Methods Enzymol v.125 Preparation, characterization and reconstitution of oxaloacetate decarboxylase from Klebsiella aerogenes, a sodium pump Dimroth, P. https://doi.org/10.1016/S0076-6879(86)25042-9
  6. Biochem. Soc. Trans. v.23 On the way towards the $Na^+$-binding site within the $F_1F_0$ ATPase of Propionigenium modestumd Dimroth, P.
  7. Proc. Natl. Acad. Sci. USA v.79 ATP-driven sodium pump in Streptococcus faecalis Heefner, D. L.;F. J. Harold https://doi.org/10.1073/pnas.79.9.2798
  8. EMBO J. v.3 Life by a new decarboxylation-dependent energy conservation mechanism with$Na^+$ as coupling ion Hilpert, W.;B. Schink;P. Dimroth
  9. Arch. Biochem. Biophys. v.244 An NADH: quinone oxidoreductase of the halotolerant bacterium Bal is specifically dependent on sodium ions Ken-Dror, S.;J. K. Lanyi;B. Schobert;B. Silver;Y. Avi-Dor https://doi.org/10.1016/0003-9861(86)90100-1
  10. J. Biocehm (Tokyo) v.109 Fluorescence quenching studies on thecharacterization of energy generated at the NADH:quinone oxidoreductase and quinol oxidase segments of marine bacteria Kim, Y. J.;S. Mizushima;H. Tokuda
  11. J. Microbiol. Biotechnol. v.6 $Na^+$-dependent NADH: uinone oxidoreductase in the respiratory chain of the marine bacterium Marinomonas vaga Kim, Y. J.;Y. Park
  12. J. Bacteriol. v.177 A novel aerobic espiratory chain-linked NADH oxidase system in Zymomonas nobilis Kim, Y. J.;K. Song;S. Rhee
  13. Biochem. Soc. Trans. v.20 The $Na^+$-translocating ATPase of Propionigenium modestum Klage, C.;W. Laubinger;P. Dimroth
  14. Alcaligenes strain 201. FEBS Lett. v.256 Respiratory-dependent orimary $Na^+$ pump in halophilic marine bacterium Kegure, K.;H. Tokuda
  15. J. Biol. Chem. v.257 Halorhodopsin is a light driven chloride pump Schobert, B.;J. K. Lanyi
  16. Biochem. Biophys. Res. Commun. v.114 Isolation of Vibro alginolyticus mutants defective in the respiration-coupled $Na^+$ pump Tokuda, H. https://doi.org/10.1016/0006-291X(83)91601-7
  17. J. Biol. Chem. v.257 Characterization of the respiration-dependent $Na^+$
  18. J. Biol. Chem. v.259 $Na^+$ is translocated at NADH: wuinone oxidoreductase segment in the respirator chanin of Vibro alginolyticus Tokuda, H.;T. Unemoto
  19. J. Bacteriol v.162 Respiration-driven $Na^+$ circulation in Vibrio parahaemolyticus Tsuchiya, T.;S. Shinoda
  20. J. Biol. Chem. v.261 Generation of $Na^+$ electrochemical potential by the $Na^+$-motive NADH oxidase and $Na^+/H^+$ antiporth system of a moderately galophilic Vibrio costicola Udagawa, T.;T. Unemoto;H. Tokuda
  21. Arch. Biochem. Biophys. v.281 Inhibition by capsaicin of NADH-quinine oxidoreductases in correlated with the presence of energycoupling site 1 in various organisms Yagi, T. https://doi.org/10.1016/0003-9861(90)90448-8