Elastic rotation of Escherichia coli FoF1 having ε subunit fused with cytochrome b562 or flavodoxin reductase
Elastic rotation of Escherichia coli FoF1 having ε subunit fused with cytochrome b562 or flavodoxin reductase
复制标题
具有与细胞色素b562或黄素氧还蛋白还原酶融合的ε亚基的大肠杆菌FoF1的弹性旋转
DOI：
10.1016/j.bbrc.2014.03.021
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
and A. Iwamoto-Kitamura
中科院分区：
文献类型：
--
作者：
5. H. Oka;H. Hosokawa;M. Nakanishi-Matsui;S. D. Dunn;M. Futai;and A. Iwamoto-Kitamura
FOF1ATP合成酶的分子内旋转使ATP的协同合成和水解成为可能。在这项研究中，使用一个小的金珠探头，我们观察到快速自转接近于没有探头时的真实速度。利用这个实验系统，我们测试了ε亚基连接到球状蛋白[细胞色素b562(ε-Cyt)或黄色素还原酶(ε-FlawR)]的FOF1的旋转，该球状蛋白明显大于中心和外围茎之间的间距。含有ε-Cyt和ε-FlawR的酶表现为连续旋转，平均速率分别为185nrps和148nrps，与野生型(172nrps)相似。然而，含有ε-Cyt或ε-FlawR的酶表现出质子转运的减少。这些结果表明，分子内的旋转是弹性的，但质子输运需要更严格的亚基/亚基相互作用。
Intra-molecular rotation of FOF1ATP synthase enables cooperative synthesis and hydrolysis of ATP. In this study, using a small gold bead probe, we observed fast rotation close to the real rate that would be exhibited without probes. Using this experimental system, we tested the rotation of FOF1with the ε subunit connected to a globular protein [cytochromeb562(ε-Cyt) or flavodoxin reductase (ε-FlavR)], which is apparently larger than the space between the central and the peripheral stalks. The enzymes containing ε-Cyt and ε-FlavR showed continual rotations with average rates of 185 and 148 rps, respectively, similar to the wild type (172 rps). However, the enzymes with ε-Cyt or ε-FlavR showed a reduced proton transport. These results indicate that the intra-molecular rotation is elastic but proton transport requires more strict subunit/subunit interaction.