Na+-dependent activation of NADH oxidase in membrane fractions from halophilic Vibrio alginolyticus and V. costicolus.
Na+-dependent activation of NADH oxidase in membrane fractions from halophilic Vibrio alginolyticus and V. costicolus.
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嗜盐弧菌和肋状弧菌膜组分中 NADH 氧化酶的 Na 依赖性激活。
DOI：
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发表时间：
1977
期刊：
影响因子：
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通讯作者：
M. Hayashi
中科院分区：
文献类型：
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作者：
T. Unemoto;M. Hayashi
轻度嗜盐海洋溶藻弧菌和中度嗜盐海洋弧菌的膜结合 NADH 氧化酶活性分别需要 0.3 和 0.5 M Na+ 才能达到最大活性；其他阳离子如Li+、K+、Rb+、Cs+、Mg2+和Ca2+作为Na+的替代品相对无效。使来自溶藻弧菌的 NADH 氧化酶产生半最大活性所需的 Na+ 浓度为 82 mN。在 400 mM K+ 和 10 mM Mg2+ 存在下，该值分别降至 6.4 和 13.8 mM，表明 K+ 和 Mg2+ 与 Na+ 协同活化。在来自肋叶弧菌的 NADH 氧化酶中也观察到了相同的阳离子依赖性模式。然而，来自非嗜盐大肠杆菌的 NADH 氧化酶对 Na+ 没有特殊要求。因此，NADH 氧化酶的 Na+ 依赖性激活似乎是这些嗜盐细菌的特征。所有检测的NADH氧化酶都受到存在的阴离子种类的影响，并且激活效果的顺序遵循溶致序列：SO4(2-)、CH3COO-大于Cl-大于NO3-大于SCN-。无论细菌来源的嗜盐性质如何，NO3- 和 SCN- 等离液阴离子都会抑制 NADH 氧化酶。
Membrane-bound NADH oxidase activities from slightly halophilic marine Vibrio alginolyticus and moderately halophilic V. costicolus required 0.3 and 0.5 M Na+, respectively, for maximum activity; other cations such as Li+,K+,Rb+,Cs+,Mg2+, and Ca2+ were relatively ineffective as replacements for Na+. The concentration of Na+ required to give half-maximum activity with the NADH oxidase from V. alginolyticus was 82 mN. This value was reduced to 6.4 and 13.8 mM in the presence of 400 mM K+ and 10 mM Mg2+, respectively, indicating that K+ and Mg2+ cooperated with Na+ for activation. The same pattern of cation dependence was observed with the NADH oxidase from V. costicolus. The NADH oxidase from nonhalophilic Escherichia coli, however, had no specific requirement for Na+. Thus, Na+-dependent activation of NADH oxidase appeared to be a characteristic feature of these halophilic bacteria. All NADH oxidases examined were influenced by the species of anion present and the order of activating effect followed the lyotropic series:SO4(2-), CH3COO- greater than Cl- greater than NO3- greater than SCN-. Chaotropic anions such as NO3- and SCN- were inhibitory to the NADH oxidases, irrespective of the halophilic nature of the bacterial source.