Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Molecular motors

What makes ATP synthase spin?

Nature volume 402, pages 247–249 (1999)Cite this article

Many years ago, when enzymes were first recognized as being proteins, few people could have imagined the wondrous, precise and diverse structures that make possible their catalytic and other functions. The ATP synthase enzyme, for example, performs catalysis as a molecular machine with an unexpected internal rotary mechanism. On page 263 of this issue, Rastogi and Girvin1 report the latest insights into this mechanism. Using sophisticated NMR and chemical probes, they have revealed structural changes in a critical subunit that could drive the rotation.

This is a preview of subscription content, access via your institution

Access options

Rent or buy this article

Get just this article for as long as you need it

$39.95

Learn more

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Model of the Escherichia coli ATP synthase.
Figure 2: How rotation of the γ subunit drives catalysis.

References

  1. Rastogi, V. K. & Girvin, M. E. Nature 402, 263–268 (1999).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Mitchell, P. & Moyle, J. Nature 213, 137–139 (1967).

    Article  ADS  CAS  PubMed  Google Scholar 

  3. Boyer, P. D. FEBS Lett. 58, 1–6 (1975).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Boyer, P. D. Annu. Rev. Biochem. 66, 717–749 (1997).

    Article  CAS  PubMed  Google Scholar 

  5. Abrahams, J. P., Leslie, A. G. W., Lutter, R. & Walker, J. E. Nature 370, 621–628 (1994).

    Article  ADS  CAS  PubMed  Google Scholar 

  6. Duncan, T. M., Bulygin, V. V., Hutcheon, M. L. & Cross, R. L. Proc. Natl Acad. Sci. USA 92, 10964–10968 (1995).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  7. Aggeler, R., Ogilvie, I. & Capaldi, R. A. J. Biol. Chem. 272, 19621–19624 (1997).

    Article  CAS  PubMed  Google Scholar 

  8. Sabbert, D., Engelbrecht, S. & Junge, W. Nature 381, 623–628 (1996).

    Article  ADS  CAS  PubMed  Google Scholar 

  9. Noji, H. et al. Nature 386, 299–302 (1997).

    Article  ADS  CAS  PubMed  Google Scholar 

  10. Dmitriev, O. Y., Jones, P. C. & Fillingame, R. H. Proc. Natl Acad. Sci. USA 96, 7785–7790 (1999).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. the Molecular Biology Institute, University of California, 611 Circle Drive East, Los Angeles, 90095-1570, California, USA

    Paul D. Boyer

Authors
  1. Paul D. Boyer
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Paul D. Boyer.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Boyer, P. What makes ATP synthase spin?. Nature 402, 247–249 (1999). https://doi.org/10.1038/46193

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/46193

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing