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Existence of a β-ionone ring-binding site in the rhodopsin molecule

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Abstract

RHODOPSIN is a carotenoid-protein, in which the 11-cis retinal chromophore, is coupled to the colourless protein, opsin. The linkage between them is a protonated Schiff base between the aldehyde group of 11-cis retinal and an ε-amino group of L-lysine in opsin1–4.

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References

  1. Bownds, D., Nature, 216, 1178–1181 (1967).

    Article  ADS  CAS  Google Scholar 

  2. Fager, R. S., Sejnowski, P., and Abrahamson, E. W., Biochem. biophys. Res. Commun., 41, 1244–1246 (1972).

    Article  Google Scholar 

  3. De Grip, W. J., Bonting, S. L., and Daemen, F. J. M., Biochim. biophys. Acta, 303, 189–193 (1973).

    Article  CAS  Google Scholar 

  4. Oseroff, A. R., and Callender, R. H., Biochemistry, 13, 4243–4248 (1974).

    Article  CAS  Google Scholar 

  5. Blatz, P., Lin, M., Balasubramaniyan, P., Balasubramaniyan, V., and Dewhurst, P. B., J. Am. chem. Soc., 91, 5930–5931 (1969).

    Article  CAS  Google Scholar 

  6. Hubbard, R., Brown, P. K., and Bownds, D., in Methods in Enzymology, 18, (edit. by McCormic, D. B., and Wright, L. D.), 615–653 (Academic, New York 1971).

    Google Scholar 

  7. Wald, G., and Brown, P. K., Nature, 177, 174–176 (1956).

    Article  ADS  CAS  Google Scholar 

  8. Sperling, W., in Biochemistry and Physiology of Visual Pigments, (edit. by Langer, H.), 19–28 (Springer, Berlin, Heidelberg, New York, 1973).

    Book  Google Scholar 

  9. Wald, G., Brown, P. K., and Smith, P. H., J. gen. Physiol., 38, 328–381 (1955).

    Article  Google Scholar 

  10. Bownds, D., and Wald, G., Nature, 205, 254–257 (1965).

    Article  ADS  CAS  Google Scholar 

  11. Matsumoto, H., Tokunaga, F., and Yoshizawa, T., Biochim. biophys. Acta, 404, 300–308 (1975).

    Article  CAS  Google Scholar 

  12. Wald, G., and Hubbard, R., in The Enzymes, second ed., 3, 369–386, (Academic, New York, 1967).

    Google Scholar 

  13. Nelson, R., deRiel, J. K., and Kropf, A., Proc. natn. Acad. Sci., U.S.A., 66, 531–538 (1970).

    Article  ADS  CAS  Google Scholar 

  14. Kropf, A., Whittenberger, B. P., Goff, S. P., and Waggoner, A. S., Expl Eye Res., 17, 591–606 (1973).

    Article  CAS  Google Scholar 

  15. Blatz, P., Dewhurst, P. B., Balasubramaniyan, V., Barasubramaniyan, P., and Lin, M., Photochem. Photobiol., 11, 1–15 (1970).

    Article  CAS  Google Scholar 

  16. Chan, W. K., Nakanishi, K., Ebrey, T. G., and Honig, B., J. Am. chem. Soc., 96, 3642–3644 (1974).

    Article  CAS  Google Scholar 

  17. Curtis, M. J., Pitt, G. A. J., and Howell, J. McC., cited in Morton, R. A., and Pitt, G. A. J., Advances in Enzymology, 32, 97–171 (Interscience, New York, 1969).

    Google Scholar 

  18. Lewin, D. R., and Thompson, J. N., Biochem. J., 103, 36p (1967).

    Article  CAS  Google Scholar 

  19. Wald, G., Fedn Proc., 12, 606 (1953).

    CAS  Google Scholar 

  20. Houghton, S. E., Lewin, D. R., and Pitt, G. A. J., cited in Morton, R. A., and Pitt, G. A. J., Advances in Enzymology, 32, 97–171 (Interscience, New York, 1969).

    Google Scholar 

  21. Azuma, M., Azuma, K., and Kito, Y., Biochim. biophys. Acta, 295, 520–527 (1973).

    Article  CAS  Google Scholar 

  22. Wald, G., Expl Eye Res., 18, 333–343 (1974).

    Article  CAS  Google Scholar 

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MATSUMOTO, H., YOSHIZAWA, T. Existence of a β-ionone ring-binding site in the rhodopsin molecule. Nature 258, 523–526 (1975). https://doi.org/10.1038/258523a0

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