IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v405y2000i6785d10.1038_35013148.html
   My bibliography  Save this article

Proton-powered turbine of a plant motor

Author

Listed:
  • 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
    Max-Planck-Institute of Molecular Cell Biology and Genetics)

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.

Suggested Citation

  • Holger Seelert & Ansgar Poetsch & Norbert A. Dencher & Andreas Engel & Henning Stahlberg & Daniel J. Müller, 2000. "Proton-powered turbine of a plant motor," Nature, Nature, vol. 405(6785), pages 418-419, May.
    • Handle: RePEc:nat:nature:v:405:y:2000:i:6785:d:10.1038_35013148
    DOI: 10.1038/35013148
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35013148
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35013148?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:405:y:2000:i:6785:d:10.1038_35013148. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.