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F₀F₁-ATP合酶的旋转催化作用。

Rotary catalysis of FoF1-ATP synthase.

作者信息

Watanabe Rikiya

机构信息

Department of Applied Chemistry, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan.

出版信息

Biophysics (Nagoya-shi). 2013 May 22;9:51-6. doi: 10.2142/biophysics.9.51. eCollection 2013.

DOI:10.2142/biophysics.9.51
PMID:27493540
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4629669/
Abstract

The synthesis of ATP, the key reaction of biological energy metabolism, is accomplished by the rotary motor protein; FoF1-ATP synthase (FoF1). In vivo, FoF1, located on the cell membrane, carries out ATP synthesis by using the proton motive force. This heterologous energy conversion is supposed to be mediated by the mechanical rotation of FoF1; however, it still remained unclear. Recently, we developed the novel experimental setup to reproduce the proton motive force in vitro and succeeded in directly observing the proton-driven rotation of FoF1. In this review, we describe the interesting working principles determined so far for FoF1 and then introduce results from our recent study.

摘要

生物能量代谢的关键反应——ATP的合成,是由旋转马达蛋白F₀F₁ - ATP合酶(F₀F₁)完成的。在体内,位于细胞膜上的F₀F₁利用质子动力势进行ATP合成。这种异源能量转换被认为是由F₀F₁的机械旋转介导的;然而,其机制仍不清楚。最近,我们开发了一种新的实验装置,用于在体外重现质子动力势,并成功地直接观察到了F₀F₁由质子驱动的旋转。在这篇综述中,我们描述了迄今为止所确定的F₀F₁有趣的工作原理,然后介绍我们最近研究的结果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/ccea6af8a5c2/9_51f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/0ebcc0735d2c/9_51f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/71137f4e2cdd/9_51f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/a5fc5f3ecfb1/9_51f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/ccea6af8a5c2/9_51f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/0ebcc0735d2c/9_51f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/71137f4e2cdd/9_51f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/a5fc5f3ecfb1/9_51f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1fb/4629669/ccea6af8a5c2/9_51f4.jpg

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本文引用的文献

1
Biased Brownian stepping rotation of FoF1-ATP synthase driven by proton motive force.质子动力势驱动的 FoF1-ATP 合酶的偏向布朗棘轮旋转。
Nat Commun. 2013;4:1631. doi: 10.1038/ncomms2631.
2
Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis.控制 F₁-ATP 酶的旋转揭示了 ATP 合成的不同和连续的结合变化。
Nat Commun. 2012;3:1022. doi: 10.1038/ncomms2026.
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Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast.比较酵母和叶绿体中的 H+-ATP 合酶的 H+/ATP 比值。
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J Biol Chem. 2012 Mar 16;287(12):9633-9. doi: 10.1074/jbc.M111.335356. Epub 2012 Jan 17.
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Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.直接观察 E. coli F₀F₁-ATP 合酶中阶梯状的类脂蛋白环旋转。
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