The origin of the sodium‐dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae

FEBS Letters

Bertsova, Yulia V¹  Bogachev, Alexander V¹ 

[1] Department of Molecular Energetics of Microorganisms, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia

关键词: Sodium translocation;    Complex I;    NADH dehydrogenase;    Klebsiella pneumoniae;    Vibrio;    CCCP;    carbonyl cyanide m-chlorophenylhydrazone;    dNADH;    reduced nicotinamide hypoxanthine dinucleotide;    NDH-1;    bacterial NADH:quinone oxidoreductase similar to mitochondrial complex I;    NDH-2;    non-coupled bacterial NADH:quinone oxidoreductase;    NQR;    bacterial NADH:quinone oxidoreductase similar to the sodium-motive NADH dehydrogenase of Vibrio;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(04)00312-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Properties of Klebsiella pneumoniae respiratory chain enzymes catalyzing NADH oxidation have been studied. Using constructed K. pneumoniae mutant strains, it was shown that three enzymes belonging to different families of NADH:quinone oxidoreductases operate in this bacterium. The NDH-2-type enzyme is not coupled with energy conservation, the NDH-1-type enzyme is a primary proton pump, and the NQR-type enzyme is homologous to the sodium-motive NADH dehydrogenase of Vibrio and is shown to be a primary Na⁺ pump. It is concluded that the NQR-type enzyme, not the NDH-1-type enzyme, catalyzes sodium-dependent NADH oxidation in K. pneumoniae.

【 授权许可】

Unknown