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单个 F(O)(F1)-ATP 合酶中的扭曲和亚基旋转。

Twisting and subunit rotation in single F(O)(F1)-ATP synthase.

机构信息

Single-Molecule Microscopy Group, Jena University Hospital, Nonnenplan 2-4, 07743 Jena, Germany.

出版信息

Philos Trans R Soc Lond B Biol Sci. 2012 Dec 24;368(1611):20120024. doi: 10.1098/rstb.2012.0024. Print 2013 Feb 5.

DOI:10.1098/rstb.2012.0024
PMID:23267178
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3538427/
Abstract

F(O)F(1)-ATP synthases are ubiquitous proton- or ion-powered membrane enzymes providing ATP for all kinds of cellular processes. The mechanochemistry of catalysis is driven by two rotary nanomotors coupled within the enzyme. Their different step sizes have been observed by single-molecule microscopy including videomicroscopy of fluctuating nanobeads attached to single enzymes and single-molecule Förster resonance energy transfer. Here we review recent developments of approaches to monitor the step size of subunit rotation and the transient elastic energy storage mechanism in single F(O)F(1)-ATP synthases.

摘要

F(O)F(1)-ATP 合酶是普遍存在的质子或离子驱动的膜酶，为各种细胞过程提供 ATP。催化的机械化学由耦合在酶内的两个旋转纳米马达驱动。通过单分子显微镜观察到了它们不同的步长，包括附着在单个酶上的波动纳米珠的视频显微镜和单分子Förster 共振能量转移。在这里，我们回顾了监测单个 F(O)F(1)-ATP 合酶中亚基旋转的步长和瞬态弹性储能机制的最新进展。

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本文引用的文献

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Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer.通过Förster共振能量转移实时检测到的单个F(o)F(1)-ATP合酶旋转双马达的弹性变形。
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