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

被引:51
作者
Bertsova, YV [1 ]
Bogachev, AV [1 ]
机构
[1] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Dept Mol Energet Microorganisms, Moscow 119899, Russia
来源
FEBS LETTERS | 2004年 / 563卷 / 1-3期
基金
俄罗斯基础研究基金会;
关键词
sodium translocation; complex I; NADH dehydrogenase; Klebsiella pneumoniae; Vibrio;
D O I
10.1016/S0014-5793(04)00312-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:207 / 212
页数:6
相关论文
共 33 条
  • [1] The pKNOCK series of broad-host-range mobilizable suicide vectors for gene knockout and targeted DNA insertion into the chromosome of Gram-negative bacteria
    Alexeyev, MF
    [J]. BIOTECHNIQUES, 1999, 26 (05) : 824 - +
  • [2] Riboflavin is a component of the Na+-pumping NADH-quinone oxidoreductase from Vibrio cholerae
    Barquera, B
    Zhou, WD
    Morgan, JE
    Gennis, RB
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (16) : 10322 - 10324
  • [3] Operation of the cbb3-type terminal oxidase in Azotobacter vinelandii
    Bertsova, YV
    Bogachev, AV
    [J]. BIOCHEMISTRY-MOSCOW, 2002, 67 (06) : 622 - 626
  • [4] Noncoupled NADH:ubiquinone oxidoreductase of Azotobacter vinelandii is required for diazotrophic growth at high oxygen concentrations
    Bertsova, YV
    Bogachev, AV
    Skulachev, VP
    [J]. JOURNAL OF BACTERIOLOGY, 2001, 183 (23) : 6869 - 6874
  • [5] Two NADH:ubiquinone oxidoreductases of Azotobacter vinelandii and their role in the respiratory protection
    Bertsova, YV
    Bogachev, AV
    Skulachev, VP
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1998, 1363 (02): : 125 - 133
  • [6] NUCLEOTIDE-SEQUENCE OF THE DMSABC OPERON ENCODING THE ANAEROBIC DIMETHYLSULFOXIDE REDUCTASE OF ESCHERICHIA-COLI
    BILOUS, PT
    COLE, ST
    ANDERSON, WF
    WEINER, JH
    [J]. MOLECULAR MICROBIOLOGY, 1988, 2 (06) : 785 - 795
  • [7] Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi
    Bogachev, AV
    Bertsova, YV
    Barquera, B
    Verkhovsky, MI
    [J]. BIOCHEMISTRY, 2001, 40 (24) : 7318 - 7323
  • [8] Kinetics of the spectral changes during reduction of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi
    Bogachev, AV
    Bertsova, YV
    Ruuge, EK
    Wikström, M
    Verkhovsky, MI
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2002, 1556 (2-3): : 113 - 120
  • [9] H+/e(-) stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells
    Bogachev, AV
    Murtazina, RA
    Skulachev, VP
    [J]. JOURNAL OF BACTERIOLOGY, 1996, 178 (21) : 6233 - 6237
  • [10] The Na+/e(-) stoichiometry of the Na+-motive NADH:quinone oxidoreductase in Vibrio alginolyticus
    Bogachev, AV
    Murtazina, RA
    Skulachev, VP
    [J]. FEBS LETTERS, 1997, 409 (03) : 475 - 477