Evidence for Conformeric States of Rhodopsin

Overview

Journal Biophys Struct Mech

Specialty Biophysics

Date 1977 Apr 21

PMID 857948

Citations 7

Authors

J G Stewart

B N Baker

T P Williams

Affiliations

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Abstract

Spectrophotometric measurements of metarhodopsin II appearance are made on five different kinds of rhodopsin preparations. Although the preparations differ greatly in their rhodopsin: phospholipid ratio, the meta II kinetics in all of them are strikingly similar in certain respects. Meta II appearance kinetics in all of the preparations are best described by two and only two exponentials. The ratio of these two rates is always about 5. The fast fraction: slow fraction ratio depends upon temperature. These fractions are reversibly convertible in the dark, and are interconverted on a time-scale which is long compared to the meta II appearance rate. It is shown that the kinetics of the earlier step in the bleaching sequence, viz., lumi-leads to meta I, is also described by double exponentials. Again the ratio of rates is ca. 5 and the fast-slow fractions correspond to those found in the meta I leads to meta II step. It is proposed that these facts support an hypothesis for the existence of two conformeric states of rhodopsin which are in thermal equilibrium. Thermodynamic parameters associated with this proposed equilibrium are presented.

Citing Articles

Conformational states and dynamics of rhodopsin in micelles and bilayers.

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Direct correlation between the R2 component of the early receptor potential and the formation of metarhodopsin II in the excised bovine retina.

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On the origin and the signal-shaping mechanism of the fast photosignal in the vertebrate retina.

Hochstrate P, Lindau M, Ruppel H Biophys J. 1982; 38(1):53-61.

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Light-induced interfacial potentials in photoreceptor membranes.

Cafiso D, Hubbell W Biophys J. 1980; 30(2):243-63.

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Spectral and kinetic evidence for the existence of two forms of bathorhodopsin.

Einterz C, Lewis J, Kliger D Proc Natl Acad Sci U S A. 1987; 84(11):3699-703.

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References

Johnson R, Williams T . Thermal stability of rhodopsin extracted with Triton X-100 surfactant. Vision Res. 1970; 10(1):85-93. DOI: 10.1016/0042-6989(70)90065-9. View

WULFF V, Adams R, Linschitz H, ABRAHAMSON E . Effect of flash illumination on rhodopsin in solution. Ann N Y Acad Sci. 1959; 74(2):281-90. DOI: 10.1111/j.1749-6632.1958.tb39551.x. View

Kim Y, Lumry R . Studies of the chymotrypsinogen family. XII. "A" type substates of alpha-chymotrypsin at neutral and alkaline pH values. J Am Chem Soc. 1971; 93(4):1003-13. DOI: 10.1021/ja00733a038. View

Hong K, Hubbell W . Preparation and properties of phospholipid bilayers containing rhodopsin. Proc Natl Acad Sci U S A. 1972; 69(9):2617-21. PMC: 427001. DOI: 10.1073/pnas.69.9.2617. View

Stewart J, Baker B, Williams T . Kinetic evidence for a conformational transition in rhodopsin. Nature. 1975; 258(5530):89-90. DOI: 10.1038/258089a0. View

von Sengbusch G, Stieve H . Flash photolysis of rhodopsin. I. Measurements on bovine rod outer segments. Z Naturforsch B. 1971; 26(5):488-9. View

GRELLMANN K, Livingston R, Pratt D . A flashphotolytic investigation of rhodopsin at low temperatures. Nature. 1962; 193:1258-60. DOI: 10.1038/1931258a0. View

Kauzmann W . Some factors in the interpretation of protein denaturation. Adv Protein Chem. 1959; 14:1-63. DOI: 10.1016/s0065-3233(08)60608-7. View

Applebury M, Zuckerman D, Lamola A, Jovin T . Rhodopsin. Purification and recombination with phospholipids assayed by the metarhodopsin I leads to metarhodopsin II transition. Biochemistry. 1974; 13(17):3448-58. DOI: 10.1021/bi00714a005. View

10.

FRENCH T, Hammes G . Relaxation spectra of ribonuclease. II. Isomerization of ribonuclease at neutral pH values. J Am Chem Soc. 1965; 87(21):4669-73. DOI: 10.1021/ja00949a002. View

11.

Williams T, Baker B, McDowell J . The influence of lipids on dynamic properties of rhodopsin. Exp Eye Res. 1974; 18(1):69-75. DOI: 10.1016/0014-4835(74)90044-x. View

12.

BLIGH E, Dyer W . A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959; 37(8):911-7. DOI: 10.1139/o59-099. View

13.

Ostroy S, Erhardt F, ABRAHAMSON E . Protein configuration changes in the photolysis of rhodopsin. II. The sequence of intermediates in thermal decay of cattle metarhodopsin in vitro. Biochim Biophys Acta. 1966; 112(2):265-77. DOI: 10.1016/0926-6585(66)90326-8. View

14.

Rapp J, Wiesenfeld J, ABRAHAMSON E . The kinetics of intermediate processes in the photolysis of bovine rhodopsin. I. A re-examination of the decay of bovine lumirhodopsin-497. Biochim Biophys Acta. 1970; 201(1):119-30. DOI: 10.1016/0304-4165(70)90017-6. View

15.

Linschitz H, WULFF V, Adams R, ABRAHAMSON E . Light-initiated changes of rhodopsin in solution. Arch Biochem Biophys. 1957; 68(1):233-6. DOI: 10.1016/0003-9861(57)90345-4. View

16.

Stewart J, Baker B, Plante E, Williams T . Effect of phospholipid removal on the kinetics of the metarhodopsin I to metarhodopsin II reaction. Arch Biochem Biophys. 1976; 172(1):246-51. DOI: 10.1016/0003-9861(76)90073-4. View