Spotlighting motors and controls of single FoF1-ATP synthase.
Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F1 structure of the Escherichia coli enzyme with the ϵ-subunit in an inhibitory conformation initiated a study for real-time monitoring of the conformational changes of ϵ. The present mini-review summarizes smFRET rotation experiments and previews new smFRET data on the conformational changes of the CTD (C-terminal domain) of ϵ in the E. coli enzyme.
*Single-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University Jena, 07743 Jena, Germany.
Michael
M
Börsch
Thomas M
TM
Duncan
D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology*; D031541:Fluorescence Resonance Energy Transfer; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry
D021122:Protein Subunits; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases