Twisting and subunit rotation in single FOF1-ATP synthase | Zendy

Hendrik Sielaff | Zendy; Michael Börsch | Zendy

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Twisting and subunit rotation in single F_OF₁-ATP synthase

Author(s) -

Hendrik Sielaff,

Michael Börsch

Publication year - 2012

Publication title -

philosophical transactions of the royal society b biological sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.753

H-Index - 272

eISSN - 1471-2970

pISSN - 0962-8436

DOI - 10.1098/rstb.2012.0024

Subject(s) - atp synthase , protein subunit , rotation (mathematics) , crystallography , chemistry , physics , microbiology and biotechnology , biology , enzyme , biochemistry , mathematics , geometry , gene

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.

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