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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Subunit rotation in Escherichia coli F_oF_1-ATP synthase during oxidative phosphorylation
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Subunit rotation in Escherichia coli F_oF_1-ATP synthase during oxidative phosphorylation

机译:氧化磷酸化过程中大肠杆菌F_oF_1-ATP合酶中的亚基旋转

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摘要

We report evidence for proton-driven sub- unit rotation in membrane-bound F_oF_1-ATP synthase during oxidative phosphorylation. A βD380C/γC87 crosslinked hy- brid F_1 having epitope-tagged βD380C subunits (βflag) exclu- sively in the two noncrosslinked positions was bound to Fo in F1-depleted membranes. After reduction of the β-γ crosslink, a brief exposure to conditions for ATP synthesis followed by reoxidation resulted in a significant amount of β_flag appearing in the β-γ crosslinked product. Such a reorientation of γC87 relative to the three β subunits can only occur through subunit rotation. Rotation was inhibited when proton transport through F_o was blocked or when ADP and Pi were omitted. These results establish F_oF_1 as the second example in nature where proton transport is coupled to subunit rotation.
机译:我们报告了膜结合的F_oF_1-ATP合酶在氧化磷酸化过程中质子驱动的亚单位旋转的证据。在两个未交联位置上都具有表位标记的βD380C亚基(β标记)的βD380C/γC87交联杂交F_1与贫F1膜中的Fo结合。 β-γ交联键还原后,短暂暴露于ATP合成条件后再氧化,导致在β-γ交联产物中出现大量β_flag。 γC87相对于三个β亚基的这种重新定向只能通过亚基旋转来实现。当质子通过F 0的传输被阻止或省略ADP和Pi时,旋转受到抑制。这些结果将F_oF_1作为质子传输与亚基旋转耦合的第二个实例。

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