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

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.

SUBMITTER: Sielaff H

PROVIDER: S-EPMC3538427 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

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

Sielaff Hendrik H Börsch Michael M

Philosophical transactions of the Royal Society of London. Series B, Biological sciences 20121224 1611

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 st ...[more]

PMID: 23267178

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