Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1982 Jun;38(3):237–241. doi: 10.1016/S0006-3495(82)84554-2

Modeling the rod outer segment birefringence change correlated with metarhodopsin II formation.

M W Kaplan
PMCID: PMC1328864  PMID: 6980674

Abstract

A rapid birefringence loss associated with metarhodopsin II formation, delta (delta n) MII, is produced when frog rod outer segments are exposed to a bleaching light flash. To analyze the nature of the underlying structure change, measurements of delta (delta n) MII were made in rod outer segments perfused with glycerol solutions to increase the refractive index of the cytoplasmic and intradisk spaces. Comparisons of experimental results with computed changes in the form birefringence component using two- and three-dielectric outer segment models for several putative structure changes were made. It is concluded that delta (delta n) MII can be due to either a change in the intrinsic birefringence component caused by the reorientation of anisotropic molecules, or to a change in the form birefringence component caused by small changes in the cytoplasmic and/or intradisk volumes.

Full text

PDF
237

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Asai H., Chiba T., Kimura S., Takagi M. A light-induced conformational change in rod photoreceptor disc membrane. Exp Eye Res. 1975 Sep;21(3):259–267. doi: 10.1016/0014-4835(75)90097-4. [DOI] [PubMed] [Google Scholar]
  2. Baumann C. Kinetics of slow thermal reactions during the bleaching of rhodopsin in the perfused frog retina. J Physiol. 1972 May;222(3):643–663. doi: 10.1113/jphysiol.1972.sp009819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blasie J. K. The location of photopigment molecules in the cross-section of frog retinal receptor disk membranes. Biophys J. 1972 Feb;12(2):191–204. doi: 10.1016/S0006-3495(72)86079-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chabre M., Breton J. Orientation of aromatic residues in rhodopsin. Rotation of one tryptophan upon the meta I to meta II transition afer illumination. Photochem Photobiol. 1979 Aug;30(2):295–299. doi: 10.1111/j.1751-1097.1979.tb07150.x. [DOI] [PubMed] [Google Scholar]
  5. Chabre M., Breton J. The orientation of the chromophore of vertebrate rhodopsin in the "meta" intermediate states and the reversibility of the meta II-meta III transition. Vision Res. 1979;19(9):1005–1018. doi: 10.1016/0042-6989(79)90226-8. [DOI] [PubMed] [Google Scholar]
  6. Chabre M., Cavaggioni A. Light induced changes in ionic flux in the retinal rod. Nat New Biol. 1973 Jul 25;244(134):118–120. doi: 10.1038/newbio244118a0. [DOI] [PubMed] [Google Scholar]
  7. Chabre M., Cavaggioni A. X-ray diffraction studies of retinal rods. II. Light effect on the osmotic properties. Biochim Biophys Acta. 1975 Mar 25;382(3):336–343. doi: 10.1016/0005-2736(75)90275-8. [DOI] [PubMed] [Google Scholar]
  8. Chabre M. Diamagnetic anisotropy and orientation of alpha helix in frog rhodopsin and meta II intermediate. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5471–5474. doi: 10.1073/pnas.75.11.5471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chabre M. X-ray diffraction studies of retinal rods. I. Structure of the disc membrane, effect of illumination. Biochim Biophys Acta. 1975 Mar 25;382(3):322–335. doi: 10.1016/0005-2736(75)90274-6. [DOI] [PubMed] [Google Scholar]
  10. Corless J. M., Kaplan M. W. Structural interpretation of the birefringence gradient in retinal rod outer segments. Biophys J. 1979 Jun;26(3):543–556. doi: 10.1016/S0006-3495(79)85270-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Corless J. M. Lamellar structure of bleached and unbleached rod photoreceptor membranes. Nature. 1972 May 26;237(5352):229–231. doi: 10.1038/237229a0. [DOI] [PubMed] [Google Scholar]
  12. Hofmann K. P., Uhl R., Hoffmann W., Kreutz W. Measurements on fast light-induced light-scattering and -absorption changes in outer segments of vertebrate light sensitive rod cells. Biophys Struct Mech. 1976 Apr 15;2(1):61–77. doi: 10.1007/BF00535653. [DOI] [PubMed] [Google Scholar]
  13. Jagger W. S., Liebman P. A. Anomalous disperison of rhodopsin in rod outer segments of the frog. J Opt Soc Am. 1976 Jan;66(1):56–59. doi: 10.1364/josa.66.000056. [DOI] [PubMed] [Google Scholar]
  14. Kaplan M. W. Concurrent birefringence and forward light-scattering measurements of flash-bleached rod outer segments. J Opt Soc Am. 1981 Dec;71(12):1467–1471. doi: 10.1364/josa.71.001467. [DOI] [PubMed] [Google Scholar]
  15. Kaplan M. W., Deffebach M. E. Birefringence measurements of structural inhomogeneities in Rana pipiens rod outer segments. Biophys J. 1978 Jul;23(1):59–70. doi: 10.1016/S0006-3495(78)85432-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kaplan M. W., Liebman P. A. Slow bleach-induced birefringence changes in rod outer segments. J Physiol. 1977 Mar;265(3):657–672. doi: 10.1113/jphysiol.1977.sp011736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Liebman P. A., Jagger W. S., Kaplan M. W., Bargoot F. G. Membrane structure changes in rod outer segments associated with rhodopsin bleaching. Nature. 1974 Sep 6;251(5470):31–36. doi: 10.1038/251031a0. [DOI] [PubMed] [Google Scholar]
  18. MATTHEWS R. G., HUBBARD R., BROWN P. K., WALD G. TAUTOMERIC FORMS OF METARHODOPSIN. J Gen Physiol. 1963 Nov;47:215–240. doi: 10.1085/jgp.47.2.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. SIDMAN R. L. The structure and concentration of solids in photoreceptor cells studied by refractometry and interference microscopy. J Biophys Biochem Cytol. 1957 Jan 25;3(1):15–30. doi: 10.1083/jcb.3.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Saibil H., Chabre M., Worcester D. Neutron diffraction studies of retinal rod outer segment membranes. Nature. 1976 Jul 22;262(5566):266–270. doi: 10.1038/262266a0. [DOI] [PubMed] [Google Scholar]
  21. THORNBURG W. The form birefringence of lamellar systems containing three or more components. J Biophys Biochem Cytol. 1957 May 25;3(3):412–419. [PMC free article] [PubMed] [Google Scholar]
  22. Uhl R., Hofmann K. P., Kreutz W. Measurement of fast light-induced disc shrinkage within bovine rod outer segments by means of a light-scattering transient. Biochim Biophys Acta. 1977 Sep 5;469(2):113–122. doi: 10.1016/0005-2736(77)90174-2. [DOI] [PubMed] [Google Scholar]
  23. Uhl R., Hofmann K. P., Kreutz W. On the light-stimulated coupling between rhodopsin and its disk membrane environment. Biochemistry. 1978 Dec 12;17(25):5347–5352. doi: 10.1021/bi00618a004. [DOI] [PubMed] [Google Scholar]
  24. Worthington C. R. Structure of photoreceptor membranes. Annu Rev Biophys Bioeng. 1974;3(0):53–80. doi: 10.1146/annurev.bb.03.060174.000413. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES