The Succinate : Quinone Oxidoreductase of Marine Bacterium Vibiro alginolyticus is a $H^+$

  • Kim, Young-Jae (Department of Microbiology, College of Natural Sciencs, Changwon National University)
  • Published : 2000.02.01

Abstract

The energetics at the succinate:quinone oxidoreductase segment of V. alginolyticus was studied using a fluorescence quenching technique with inside-out membrane vesicles. A transient generation of the membrane potential (inside-positive) and ${\Delta}pH$ (inside-acidic) occurred in the presence of KCN and succinate when ubiquinone-1 (Q1) was added. The membrane potential (\Delta\psi$) generated by the succinate; quinone oxidoreductase segment was completely collapsed by the protonophore carbonylcyanide m-chlorophenylhydrazone (CCCP) and the membrane permeable anion $SCN^{-}$, whereas the ${\Delta}pH$ was completely collapsed by CCCP and $(NH_4)_2SO_4$. From these results, it was concluded that the succinate: quinone oxidoreductase segment as well as quinol oxidase [1] in the respiratory chain of V. alginolyticus generated $H^{+}$ electrochemical potential.

Keywords

References

  1. J. Biochem. v.109 Fluorescence quenching studies on the characterization of energy generated at the NADH:quione oxidoreductase and quinol oxidase segments of marine bacteria. Kim, Y. J.;S. Mizushima;H. Tokuda
  2. Biochemistry v.26 NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Matsushita, K.;T. Ohnishi;H. R. Kaback
  3. Biochim. Biophys. Acta v.1016 Δψ and ΔpH generation by the $H^+$ pumps of the respiratory chain and ATPase in subcellular vesicles from marine bacterium Vibrio alginolyticus. Smirnova, I. A.;M. L. Vaghina;V. A. Kostyrko.
  4. Biochem. Biophys. Res. Commun. v.114 Isolation of Vibrio alginolyticus mutants defective in the respiration-coupled $Na^+$ pump. Tokuda, H.
  5. J. Biol. Chem. v.259 $Na^+$ is translocated at NADH:quinone oxidoreductase segment in the respiratory chain of Vibrio alginolyticus. Tokuda, H.;T. Unemoto.