Stepping rotation of F 1 -ATPase visualized through angle-resolved single-fluorophore imaging
Open Access
- 6 June 2000
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 97 (13) , 7243-7247
- https://doi.org/10.1073/pnas.120174297
Abstract
Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F1-ATPase revealed that the subunit rotates in the molecule in discrete 120° steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120° stepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.Keywords
This publication has 29 references indexed in Scilit:
- Single‐fluorophore imaging with an unmodified epifluorescence microscope and conventional video cameraJournal of Microscopy, 1999
- F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° StepsCell, 1998
- Three‐stepped rotation of subunits γ and ϵ in single molecules of F‐ATPase as revealed by polarized, confocal fluorometryFEBS Letters, 1998
- Those Blinking Single MoleculesScience, 1997
- Rotation of a γ-ε Subunit Domain in the Escherichia coli F1F0-ATP Synthase ComplexJournal of Biological Chemistry, 1997
- Catalytic Activity of the α3β3γ Complex of F1-ATPase without Noncatalytic Nucleotide Binding SitePublished by Elsevier ,1997
- Analysis of time-dependent change of Escherichia coli Fl-ATPase activity and its relationship with apparent negative cooperativityBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1995
- Single-Molecule Detection by Laser-Induced Fluorescence Technique with a Position-Sensitive Photon-Counting ApparatusJapanese Journal of Applied Physics, 1994
- Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assayJournal of Molecular Biology, 1990
- The loose coupling mechanism in molecular machines of living cellsAdvances in Biophysics, 1986