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- W2140328121 endingPage "20120024" @default.
- W2140328121 startingPage "20120024" @default.
- W2140328121 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." @default.
- W2140328121 created "2016-06-24" @default.
- W2140328121 creator A5044178079 @default.
- W2140328121 creator A5050374500 @default.
- W2140328121 date "2013-02-05" @default.
- W2140328121 modified "2023-10-17" @default.
- W2140328121 title "Twisting and subunit rotation in single F<sub>O</sub>F<sub>1</sub>-ATP synthase" @default.
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