Proton-powered turbine of a plant motor

Holger Seelert, Ansgar Poetsch, Norbert A. Dencher (), Andreas Engel, Henning Stahlberg and Daniel J. Müller
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Holger Seelert: Physical Biochemistry, Darmstadt University of Technology
Ansgar Poetsch: Physical Biochemistry, Darmstadt University of Technology
Norbert A. Dencher: Physical Biochemistry, Darmstadt University of Technology
Andreas Engel: M. E. Müller-Institute for Structural Biology, Biozentrum, University of Basel
Henning Stahlberg: M. E. Müller-Institute for Structural Biology, Biozentrum, University of Basel
Daniel J. Müller: M. E. Müller-Institute for Structural Biology, Biozentrum, University of Basel

Nature, 2000, vol. 405, issue 6785, 418-419

Abstract: Abstract ATP synthases are enzymes that can work in two directions to catalyse either the synthesis or breakdown of ATP, and they constitute the smallest rotary motors in biology. The flow of protons propels the rotation1 of a membrane-spanning complex of identical protein subunits, the number of which determines the efficiency of energy conversion. This proton-powered turbine is predicted to consist of 12 subunits2,3,4, based on data for Escherichia coli5. The yeast mitochondrial enzyme, however, has only 10 subunits6. We have imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, find that its turbine has 14 subunits, arranged in a cylindrical ring.

Date: 2000
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DOI: 10.1038/35013148

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