Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1975 Dec;15(12):1181–1200. doi: 10.1016/S0006-3495(75)85894-2

The electric dipole moment of rhodopsin solubilized in Triton X-100.

D C Petersen, R A Cone
PMCID: PMC1334802  PMID: 1203446

Abstract

The electric dipole moment of solubilized rhodopsin was determined with dielectric dispersion measurements. Rhodopsin was extracted from disc membranes of cattle rod outer segments with the nonionic detergent Triton X-100. The dipole moment of rhodopsin at its isoionic point in the detergent micelle is 720 D (150 charge-A). This value is comparable to dipole moments of nonmembrane proteins, especially those which tend to aggregate or polymerize. Flash irradiation of the rhodopsin results in an increase in the dipole moment of about 25 D (5 charge-A). The light-induced increase in dipole moment appears to be composed of two parts--a faster component related to a change in the number of protons bound by rhodopsin and a slower component apparently independent of the change in proton binding.

Full text

PDF
1181

Selected References

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

  1. ALBRECHT G. Terminal amino acids of rhodopsin. J Biol Chem. 1957 Nov;229(1):477–487. [PubMed] [Google Scholar]
  2. AMES B. N., DUBIN D. T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem. 1960 Mar;235:769–775. [PubMed] [Google Scholar]
  3. Applequist J., Mahr T. G. The conformation of poly-L-tyrosine in quinoline from dielectric dispersion studies. J Am Chem Soc. 1966 Dec 5;88(23):5419–5429. doi: 10.1021/ja00975a010. [DOI] [PubMed] [Google Scholar]
  4. Bridges C. D. The molar absorbance coefficient of rhodopsin. Vision Res. 1971 Aug;11(8):841–848. doi: 10.1016/0042-6989(71)90006-x. [DOI] [PubMed] [Google Scholar]
  5. Burke M. J., Pratt D. C., Faulkner T. R., Moscowitz A. An analysis of the absorption and circular dichroism of some visual pigments. Exp Eye Res. 1973 Dec 24;17(6):557–572. doi: 10.1016/0014-4835(73)90085-7. [DOI] [PubMed] [Google Scholar]
  6. Cone R. A. Early receptor potential: photoreversible charge displacement in rhodopsin. Science. 1967 Mar 3;155(3766):1128–1131. doi: 10.1126/science.155.3766.1128. [DOI] [PubMed] [Google Scholar]
  7. Crescitelli F. Extraction of visual pigments with certain alkyl phenoxy polyethoxy ethanol surface-active compounds. Vision Res. 1967 Sep;7(9):685–693. doi: 10.1016/0042-6989(67)90032-6. [DOI] [PubMed] [Google Scholar]
  8. Cummins H. Z., Carlson F. D., Herbert T. J., Woods G. Translational and rotational diffusion constants of tobacco mosaic virus from Rayleigh linewidths. Biophys J. 1969 Apr;9(4):518–546. doi: 10.1016/S0006-3495(69)86402-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Daemen F. J., Borggreven J. M., Bonting S. L. Molar absorbance of cattle rhodopsin. Nature. 1970 Sep 19;227(5264):1259–1260. doi: 10.1038/2271259a0. [DOI] [PubMed] [Google Scholar]
  10. Daemen F. J. Vertebrate rod outer segment membranes. Biochim Biophys Acta. 1973 Nov 28;300(3):255–288. doi: 10.1016/0304-4157(73)90006-3. [DOI] [PubMed] [Google Scholar]
  11. Emrich H. M. Optical measurements of the rapid pH-change in the visual process during the metarhodopsin I-II reaction. Z Naturforsch B. 1971 Apr;26(4):352–356. doi: 10.1515/znb-1971-0417. [DOI] [PubMed] [Google Scholar]
  12. FUKAMI I. On the electrophoresis of cattle rhodopsin. Jpn J Physiol. 1960 Dec 15;10:666–672. doi: 10.2170/jjphysiol.10.666. [DOI] [PubMed] [Google Scholar]
  13. Falk G., Fatt P. Rapid hydrogen ion uptake of rod outer segments and rhodopsin solutions on illumination. J Physiol. 1966 Mar;183(1):211–224. doi: 10.1113/jphysiol.1966.sp007861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Gerber B. R., Routledge L. M., Takashima S. Self-assembly of bacterial flagellar protein: dielectric behavior of monomers and polymers. J Mol Biol. 1972 Nov 14;71(2):317–337. doi: 10.1016/0022-2836(72)90354-3. [DOI] [PubMed] [Google Scholar]
  15. HARA R. CHANGES IN ELECTRICAL CONDUCTANCE OF RHODOPSIN ON PHOTOLYSIS. J Gen Physiol. 1963 Nov;47:241–264. doi: 10.1085/jgp.47.2.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. HARA T. The effect of illumination on the electrical conductance of rhodopsin solutions. J Gen Physiol. 1958 May 20;41(5):857–877. doi: 10.1085/jgp.41.5.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hagins W. A., McGaughy R. E. Molecular and thermal origins of fast photoelectric effects in the squid retina. Science. 1967 Aug 18;157(3790):813–816. doi: 10.1126/science.157.3790.813. [DOI] [PubMed] [Google Scholar]
  18. Hagins W. A., Rüppel H. Fast photoelectric effects and the properties of vertebrate photoreceptors as electric cables. Fed Proc. 1971 Jan-Feb;30(1):64–68. [PubMed] [Google Scholar]
  19. Heitzmann H. Rhodopsin is the predominant protein of rod outer segment membranes. Nat New Biol. 1972 Jan 26;235(56):114–114. doi: 10.1038/newbio235114a0. [DOI] [PubMed] [Google Scholar]
  20. Heller J., Ostwald T. Rhodopsin: conformational changes in a membrane protein. Ann N Y Acad Sci. 1972 Jun 20;195:439–449. [PubMed] [Google Scholar]
  21. Heller J. Structure of visual pigments. I. Purification, molecular weight, and composition of bovine visual pigment500. Biochemistry. 1968 Aug;7(8):2906–2913. doi: 10.1021/bi00848a030. [DOI] [PubMed] [Google Scholar]
  22. Hendrickx H., Verbruggen R., Rosseneu-Motreff M. Y., Blaton V., Peeters H. The dipolar origin of protein relaxation. Biochem J. 1968 Dec;110(3):419–424. doi: 10.1042/bj1100419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Hubbard R., Bownds D., Yoshizawa T. The chemistry of visual photoreception. Cold Spring Harb Symp Quant Biol. 1965;30:301–315. doi: 10.1101/sqb.1965.030.01.032. [DOI] [PubMed] [Google Scholar]
  24. Incardona N. L., Miles K., Baker B. N. Sedimentation of bovine rhodopsin--digitonin micelles. Nat New Biol. 1971 Feb 24;229(8):250–252. doi: 10.1038/newbio229250a0. [DOI] [PubMed] [Google Scholar]
  25. Irreverre F., Stone A. L., Shichi H., Lewis M. S. Biochemistry of visual pigments. I. Purification and properties of bovine rhodopsin. J Biol Chem. 1969 Feb 25;244(4):529–536. [PubMed] [Google Scholar]
  26. Johnson R. H., Williams T. P. Thermal stability of rhodopsin extracted with Triton X-100 surfactant. Vision Res. 1970 Jan;10(1):85–93. doi: 10.1016/0042-6989(70)90065-9. [DOI] [PubMed] [Google Scholar]
  27. Kirkwood J. G., Shumaker J. B. The Influence of Dipole Moment Fluctuations on the Dielectric Increment of Proteins in Solution. Proc Natl Acad Sci U S A. 1952 Oct;38(10):855–862. doi: 10.1073/pnas.38.10.855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Lewis M. S., Krieg L. C., Kirk W. D. The molecular weight and detergent binding of bovine rhodopsin. Exp Eye Res. 1974 Jan;18(1):29–40. doi: 10.1016/0014-4835(74)90041-4. [DOI] [PubMed] [Google Scholar]
  29. 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]
  30. Murakami M., Pak W. L. Intracellularly recorded early receptor potential of the vertebrate photoreceptors. Vision Res. 1970 Oct;10(10):965–975. doi: 10.1016/0042-6989(70)90074-x. [DOI] [PubMed] [Google Scholar]
  31. RADDING C. M., WALD G. Acid-base properties of rhodopsin and opsin. J Gen Physiol. 1956 Jul 20;39(6):909–922. doi: 10.1085/jgp.39.6.909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Rosseneu-Motreff M. Y., Soetewey F., Lamote R., Peeters H. Size and shape determination of apotransferrin and transferrin monomers. Biopolymers. 1971 Jun;10(6):1039–1048. doi: 10.1002/bip.360100610. [DOI] [PubMed] [Google Scholar]
  33. SCHWAN H. P. Electrical properties of tissue and cell suspensions. Adv Biol Med Phys. 1957;5:147–209. doi: 10.1016/b978-1-4832-3111-2.50008-0. [DOI] [PubMed] [Google Scholar]
  34. Scheider W. Dielectric Relaxation of Molecules with Fluctuating Dipole Moment. Biophys J. 1965 Sep;5(5):617–628. doi: 10.1016/s0006-3495(65)86740-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Sengbusch G. V., Stieve H. Flash photolysis of rhodopsin. II. Measurements on rhodopsin digitonin solutions and fragments of rod outer segments. Z Naturforsch B. 1971 Aug;26(8):861–862. doi: 10.1515/znb-1971-0830. [DOI] [PubMed] [Google Scholar]
  36. Shichi H. Spectrum and purity of bovine rhodopsin. Biochemistry. 1970 Apr 28;9(9):1973–1977. doi: 10.1021/bi00811a018. [DOI] [PubMed] [Google Scholar]
  37. Shields J. E., Dinovo E. C., Henriksen R. A., Kimbel R. L., Jr, Millar P. G. The purification and amino acid composition of bovine rhodopsin. Biochim Biophys Acta. 1967 Oct 23;147(2):238–251. doi: 10.1016/0005-2795(67)90402-3. [DOI] [PubMed] [Google Scholar]
  38. Soetewey F., Rosseneu-Motreff M., Lamote R., Peeters H. Size and shape determination of native and defatted bovine serum albumin monomers. II. Influence of the fatty acid content on the conformation of bovine serum albumin monomers. J Biochem. 1972 Apr;71(4):705–710. [PubMed] [Google Scholar]
  39. TAKASHIMA S. DIELECTRIC DISPERSION OF ALBUMINS. STUDIES OF DENATURATION BY DIELECTRIC MEASUREMENT. Biochim Biophys Acta. 1964 May 25;79:531–538. doi: 10.1016/0926-6577(64)90218-9. [DOI] [PubMed] [Google Scholar]
  40. WALD G., BROWN P. K. The molar extinction of rhodopsin. J Gen Physiol. 1953 Nov 20;37(2):189–200. doi: 10.1085/jgp.37.2.189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Wald G., Brown P. K. The Synthesis of Rhodopsin from Retinene(1). Proc Natl Acad Sci U S A. 1950 Feb;36(2):84–92. doi: 10.1073/pnas.36.2.84. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Wong J. K., Ostroy S. E. Hydrogen ion changes of rhodopsin I. Proton uptake during the metarhodopsin I 478 metarhodopsin II 308 reaction. Arch Biochem Biophys. 1973 Jan;154(1):1–7. doi: 10.1016/0003-9861(73)90028-3. [DOI] [PubMed] [Google Scholar]
  43. Wu C. W., Stryer L. Proximity relationships in rhodopsin. Proc Natl Acad Sci U S A. 1972 May;69(5):1104–1108. doi: 10.1073/pnas.69.5.1104. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Zorn M., Futterman S. Properties of rhodopsin dependent on associated phospholipid. J Biol Chem. 1971 Feb 25;246(4):881–886. [PubMed] [Google Scholar]
  45. von Sengbusch G., Stieve H. Flash photolysis of rhodopsin. I. Measurements on bovine rod outer segments. Z Naturforsch B. 1971 May;26(5):488–489. [PubMed] [Google Scholar]

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

RESOURCES