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Respiratory Chain-Linked Components of the Marine Bacterium Vibrio alginolyticus Affect Each Other  

Kim, Young-Jae (Department of Microbiology, College of Natural Sciences, Changwon Natioal University, Sarim-dong, Changwon, Kyungnam 641-773,)
Publication Information
Journal of Microbiology / v.40, no.2, 2002 , pp. 125-128 More about this Journal
Abstract
The aerobic respiratory chain of Vibrio alginolyticus possesses two different kinds of NADH oxidase systems, i.e., an $Na^{+}$-dependent NADH oxidase system and an $Na^{+}$-independent NADH oxidase system. When deamino-NADH, which is the only substrate for the $Na^{+}$-dependent NADH oxidase system, was used as a substrate, the maximum activities of $N^{+}$-dependent NADH: quinone oxidoreductase and $Na^{+}$-dependent NADH oxidase were obtained at about 0.06 M and 0.2 M NaCl, respectively. When NADH, which is a substrate for both $Na^{+}$-dependent and $Na^{+}$-independent NADH oxidase systems was used as a substrate, the NADH oxidase activity had a pH optimum at about 8.0. In cGntrastl when deamino-NADH was used as a substrate, the NADH oxidase activity had a pH optimum at about 9.0. On the other handle inside-out membrane vesicles prepared from the wild-type bacterium generated only a very small $\Delta$pH by the NADH oxidase system, whereas inside-out membrane vesicles prepared from Napl, which is a mutant defective in the $Na^{+}$ pump, generated $\Delta$pH to a considerable extent by the NADH oxidase system. On the basis of the results\ulcorner it was concluded that the respiratory chain-linked components of V. atginotyticus affect each other.
Keywords
The aerobic respiratory chain of Vibrio alginolyticus possesses two different kinds of NADH oxidase systems, i.e., an $Na^{+}$-dependent NADH oxidase system and an $Na^{+}$-independent NADH oxidase system. When deamino-NADH, which is the only substrate for the $Na^{+}$-dependent NADH oxidase system, was used as a substrate, the maximum activities of $N^{+}$-dependent NADH: quinone oxidoreductase and $Na^{+}$-dependent NADH oxidase were obtained at about 0.06 M and 0.2 M NaCl, respectively;
Citations & Related Records

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연도 인용수 순위
1 Generation of the electrochemical potential of Na+ by the Na+ -motive NADH oxidase in inverted membrane vesicles of Vibrio alginolyticus /
[ Tokuda, H.;T. Udagawa;T. Unemoto ] / FEBS Lett   DOI   ScienceOn
2 Characterization of the respiration-dependent Na+ pump in the marine bacterium Vibrio alginolyticus /
[ Tokuda, H.;T. Unemoto ] / J. Biol. Chem.
3 Fluorescence quenching studies on the characterization of energy generated at the NADH: quinone oxidoreductase and quinol oxidase segments of marine bacteria /
[ Kim, Y.J.;S. Mizushima;H. Tokuda ] / J. Biochem.   DOI
4 Respiratory Na+ pump and Na+ -dependent energetics in Vibrio alginolyticus /
[ Tokuda, H. ] / J. Bioenerg. Biomembr.   DOI
5 Na+ is translocated at NADH: quinone oxidoreductase segment in the respiratoy chain of Vibrio alginolyticus /
[ Tokuda, H.;T. Unemoto ] / J. Biol. Chem.
6 Isolation of Vibrio alginolyticus mutants defective in the respiration-coupled Na+ pump /
[ Tokuda, H. ] / Biochem. Biophys. Res. Commun.   DOI   ScienceOn
7 Sodium translocation by NADH oxidase of Vibro alginolyticus: Isolation and characterization of the sodium pump-defective mutants /
[ Tokuda, H. ] / Methods Enzymol   DOI