Skip to main content
Log in

Kinetic evidence for a conformational transition in rhodopsin

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

AFTER light absorption, rhodopsin decays through a series of spontaneous reactions1,10, the kinetics of which have been the object of considerable study. In a variety of conditions the decay kinetics of bathorhodopsin (prelumirhodopsin), lumirhodopsin, and metarhodopsin I (meta I) have been found to be non-first order, but are consistent with a set of parallel, independent first-order reactions2–10. These kinetics have been assumed to result from the existence of multiple forms of each of these intermediates, and it has been proposed that rhodopsin itself exists in different forms or different environments in some conditions7. The kinetics of meta I→ meta II in both dodecyltrimethylammonium bromide- and digitonin-solubilised phospholipid-free rhodopsin are also consistent with two forms of meta I which decay independently (J. G. S. and E. O. Plante, unpublished). We show here that the effect of temperature changes on these kinetics is consistent with the hypothesis that rhodopsin exists in two forms in equilibrium resulting from the accessibility of two stable conformational states separated by a small difference in free energy.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Matthews, R. G., Hubbard, R., Brown, P. K., and Wald, G., J. gen. Physiol., 47, 215–240 (1963).

    Article  CAS  Google Scholar 

  2. Linschitz, H., Wulff, V. J., Adams, R. G., and Abrahamson, E. W., Archs biochem. Biophys., 68, 233–236 (1957).

    Article  CAS  Google Scholar 

  3. Wulff, V. J., Adams, R. G., Linschitz, H., and Abrahamson, E. W., Ann. N.Y. Acad. Sci., 74, 281–290 (1958).

    Article  ADS  CAS  Google Scholar 

  4. Abrahamson, E. W., Marquisee, J., Gavuzzi, P., and Roubie, J., Z. Elektrochem., 64, 177–180 (1960).

    CAS  Google Scholar 

  5. Grellmann, K-H., Livingston, R., and Pratt, D., Nature, 193, 1258–1260 (1962),

    Article  ADS  CAS  Google Scholar 

  6. Pratt, D. C., Livingston, R., and Grellmann, K-H., Photochem. Photobiol., 3, 121–127 (1964).

    Article  CAS  Google Scholar 

  7. Marquisee, J., thesis, Case Western Reserve Univ., Cleveland, Ohio (1966).

  8. Rapp, J., Wiesenfeld, J. R., and Abrahamson, E. W., Biochim. biophys. Acta, 201, 119–130 (1970).

    Article  CAS  Google Scholar 

  9. Williams, T. P., Baker, B. N., and McDowell, J. H., Expl Eye Res., 18 69–75 (1974).

    Article  CAS  Google Scholar 

  10. Applebury, M. L., Zuckerman, D. M., Lamola, A. A., and Jovin, T. M., Biochemistry, 13, 3448–3458 (1974).

    Article  CAS  Google Scholar 

  11. Lumry, R., and Biltonen, R., in Structure and Stability of Biological Macromolecules (edit. by Timasheff, S., and Fasman F.), (Dekker, New York, 1969).

    Google Scholar 

  12. Kim, Y. D., and Lumry, R., J. Am. chem. Soc., 93, 1003–1013 (1971).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

STEWART, J., BAKER, B. & WILLIAMS, T. Kinetic evidence for a conformational transition in rhodopsin. Nature 258, 89–90 (1975). https://doi.org/10.1038/258089a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/258089a0

  • Springer Nature Limited

This article is cited by

Navigation