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Microscopy of single FoF1-ATP synthases— The unraveling of motors, gears, and controls
Article first published online: 4 FEB 2013
Copyright © 2013 International Union of Biochemistry and Molecular Biology, Inc.
Volume 65, Issue 3, pages 227–237, March 2013
How to Cite
Börsch, M. (2013), Microscopy of single FoF1-ATP synthases— The unraveling of motors, gears, and controls. IUBMB Life, 65: 227–237. doi: 10.1002/iub.1149
- Issue published online: 25 FEB 2013
- Article first published online: 4 FEB 2013
- Manuscript Accepted: 12 JAN 2013
- Manuscript Received: 11 DEC 2012
- enzyme mechanisms;
- membrane proteins;
- structural biology
Optical microscopy of single F1-ATPase and FoF1-ATP synthases started 15 years ago. Direct demonstration of ATP-driven subunit rotation by videomicroscopy became the new exciting tool to analyze the conformational changes of this enzyme during catalysis. Stimulated by these experiments, technical improvements for higher time resolution, better angular resolution, and reduced viscous drag were developed rapidly. Optics and single-molecule enzymology were entangled to benefit both biochemists and microscopists. Today, several single-molecule microscopy methods are established including controls for the precise nanomanipulation of individual enzymes in vitro. Förster resonance energy transfer, which has been used for simultaneous monitoring of conformational changes of different parts of this rotary motor, is one of them and may become the tool for the analysis of single FoF1-ATP synthases in membranes of living cells. Here, breakthrough experiments are critically reviewed and challenges are discussed for the future microscopy of single ATP synthesizing enzymes at work. © 2013 IUBMB Life, 65(3):227–237, 2013