title: 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.
authors.affiliation: Single-Molecule Microscopy Group, Jena University Hospital, Nonnenplan 2-4, 07743 Jena, Germany.
authors.forename: Hendrik
authors.initials: H
authors.lastname: Sielaff
authors.forename: Michael
authors.initials: M
authors.lastname: Börsch
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D000465:Algorithms; D002384:Catalysis; D002462:Cell Membrane / Q000737:chemistry; D019295:Computational Biology; D003198:Computer Simulation; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008164:Luminescent Proteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D026901:Membrane Transport Proteins / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D018715:Microscopy, Video; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012399:Rotation
chemical_list: D029968:Escherichia coli Proteins; D008164:Luminescent Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D011993:Recombinant Fusion Proteins; C499697:TatA protein, E coli; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases