| Literature DB >> 23267178 |
Hendrik Sielaff1, Michael Börsch.
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.Entities:
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Year: 2012 PMID: 23267178 PMCID: PMC3538427 DOI: 10.1098/rstb.2012.0024
Source DB: PubMed Journal: Philos Trans R Soc Lond B Biol Sci ISSN: 0962-8436 Impact factor: 6.237