The Journal of Membrane Biology

, Volume 43, Issue 2–3, pp 277–294 | Cite as

Comparative studies on the fine structure of purple membrane fromHalobacterium cutirubrum andHalobacterium halobium

  • G. K. Papadopoulos
  • D. D. Muccio
  • T. L. Hsiao
  • J. Y. Cassim
Article

Summary

Direct comparison of the absorption and circular dichroic spectra of dark- and light-adapted purple membrane fromHalobacterium cutirubrum andHalobacterium halobium indicated no apparent species differences. In addition, sequential bleaching and regeneration of the purple membrane with concomitant monitoring of the absorption and circular dichroic spectra showed no species differences as well. Furthermore, perturbation of the structure of the purple membrane from either species with a detergent, Triton X-100, yielded similar spectral changes. It was concluded: (i) no apparent differences exist in the molecular organization and protein fine structure of the two purple membranes, (ii) if exciton interaction among the retinal chromophores is a reasonable possibility in the case of the purple membrane fromHalobacterium halobium, it must be similarly so for the membrane fromHalobacterium cutirubrum, (iii) the effects of light adaptation on the membrane structure of both species are essentially the same, and (iv) the underlying molecular mechanisms for the bleaching and regenerative processes must be similar, if not identical, for the purple membranes of the two species.

Keywords

Human Physiology Fine Structure Regenerative Process Membrane Structure Apparent Difference 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Bauer, P.J., Dencher, N.A., Heyn, M.P. 1976. Evidence for chromophore-chromophore interactions in the purple membrane from reconstitution experiments of the chromophore-free membrane.Biophys. Struct. Mechan. 2:79Google Scholar
  2. 2.
    Becher, B., Cassim, J.Y. 1975. Effects of light perturbation on the circular dichroism of purple membrane fromHalobacterium halobium.Biophys. J. 15:66a (Abstr.)Google Scholar
  3. 3.
    Becher, B., Cassim, J.Y. 1975. Improved isolation procedures for the purple membrane ofHalobacterium halobium.Prep. Biochem. 5:161PubMedGoogle Scholar
  4. 4.
    Becher, B., Cassim, J.Y. 1976. Effects of light adaptation on the purple membrane structure ofHalobacterium halobium.Biophys. J. 16:1183PubMedGoogle Scholar
  5. 5.
    Becher, B., Cassim, J.Y. 1977. Effects of bleaching and regeneration on the purple membrane structure ofHalobacterium halobium.Biophys. J. 19:285PubMedGoogle Scholar
  6. 6.
    Becher, B., Ebrey, T.G. 1976. Evidence for chromophore-chromophore (exciton) interaction in the purple membrane ofHalobacterium halobium.Biochem. Biophys. Res. Commun. 69:1PubMedGoogle Scholar
  7. 7.
    Blaurock, A.E., Stoeckenius, W. 1971. Structure of the purple membrane.Nature New Biol. 233:152PubMedGoogle Scholar
  8. 8.
    Blaurock, A.E. 1975. Bacteriorhodopsin: A transmembrane pump containing α-helix.J. Mol. Biol. 93:139PubMedGoogle Scholar
  9. 9.
    Bradley, D.F., Tinoco, I., Jr., Woody, R.W. 1963. Absorption and rotation of light by helical oligomers: The nearest neighbor approximation.Biopolymers 1:239Google Scholar
  10. 10.
    Cassim, J.Y., Lin, T.I. 1975. Does myosin-substrate interactionin vitro result in a delocalized conformation change?J. Supramol. Struct. 3:510PubMedGoogle Scholar
  11. 11.
    Chignell, C.F., Chignell, D.A. 1975. A spin label study of purple membranes fromHalobacterium halobium.Biochem. Biophys. Res. Commun. 62:136PubMedGoogle Scholar
  12. 12.
    Henderson, R. 1975. The structure of purple membrane fromHalobacterium halobium: Analysis of the X-ray diffraction pattern.J. Mol. Biol. 93:123PubMedGoogle Scholar
  13. 13.
    Henderson, R. 1977. The purple membrane fromHalobacterium halobium.Annu. Rev. Biophys. Bioeng. 6:87PubMedGoogle Scholar
  14. 14.
    Henderson, R., Unwin, P.N.T. 1975. Three-dimensional model of purple membrane obtained by electron microscopy.Nature (London) 257:28Google Scholar
  15. 15.
    Heyn, M.P., Bauer, P.J., Dencher, N.A. 1975. A natural CD label to probe the structure of the purple membrane fromHalobacterium halobium by means of exciton coupling effects.Biochem. Biophys. Res. Commun. 67:897PubMedGoogle Scholar
  16. 16.
    Jan, L.Y. 1975. The isomeric configuration of the bacteriorhodopsin chromophore.Vision Res. 15:1081PubMedGoogle Scholar
  17. 17.
    Kushwaha, S.C., Kates, M. 1973. Isolation and identification of minor C40-carotenoids inHalobacterium cutirubrum.Biochim. Biophys. Acta 316:235PubMedGoogle Scholar
  18. 18.
    Kushwaha, S.C., Kates, M., Martin, W.G. 1975. Characterization and composition of purple and red membrane ofHalobacterium cutirubrum.Can. J. Biochem. 53:284PubMedGoogle Scholar
  19. 19.
    Kushwaha, S.C., Kates, M., Stoeckenius, W. 1976. Comparison of purple membrane fromHalobacterium halobium andHalobacterium cutirubrum.Biochim. Biophys. Acta 426:703PubMedGoogle Scholar
  20. 20.
    Oesterhelt, D., Meentzen, M., Schulman, L. 1973. Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans retinal as its chromophores.Eur. J. Biochem. 40:453PubMedGoogle Scholar
  21. 21.
    Oesterhelt, D., Stoeckenius, W. 1971. Rhodopsin-like protein from the purple membrane ofHalobacterium halobium.Nature New Biol. 233:149PubMedGoogle Scholar
  22. 22.
    Oesterhelt, D., Stoeckenius, W. 1973. Functions of a new photoreceptor membrane.Proc. Nat. Acad. Sci. USA 70:2853PubMedGoogle Scholar
  23. 23.
    Papadopoulos, G.K., Hsiao, T.L., Cassim, J.Y. 1978. Determination of the retinal/protein molar ratios for the purple membranes ofHalobacterium halobium andHalobacterium cutirubrum.Biochem. Biophys. Res. Commun. 81:127PubMedGoogle Scholar
  24. 24.
    Pettei, M.J., Yudd, A.P., Nakanishi, K., Henselman, R., Stoeckenius, W. 1977. Identification of retinal isomers isolated from bacteriorhodopsin.Biochemistry 16:1955PubMedGoogle Scholar
  25. 25.
    Reynolds, J., Stoeckenius, W. 1977. Molecular weight of bacteriorhodopsin solubilized in Triton X-100.Proc. Nat. Acad. Sci. USA 74:2803PubMedGoogle Scholar
  26. 26.
    Urry, D.W., Masotti, L., Krivacic, J.R. 1971. Circular dichroism of biological membranes.Biochem. Biophys. Acta 241:600PubMedGoogle Scholar

Copyright information

© Springer-Verlag New York Inc. 1978

Authors and Affiliations

  • G. K. Papadopoulos
    • 1
  • D. D. Muccio
    • 1
  • T. L. Hsiao
    • 1
  • J. Y. Cassim
    • 1
  1. 1.Department of Microbiology and Division of Sensory Biophysics, College of Biological SciencesThe Ohio State UniversityColumbus

Personalised recommendations