Rhodopsin structure and function

Biomembranes: A Multi-Volume Treatise

Volumn 2, Issue C, 1996, Pages 1-32

  J Litman, Burton ^a   C Mitchell, Drake ^a  

^a NONE

Author keywords

[No Author keywords available]

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EID: 7044233192     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(07)80004-3     Document Type: Article

References (144)

1. Akhtar M., Blosse P.T., and Dewhurst P.B. The reduction of a rhodopsin derivative. Life Sci. 4 (1965) 1221-1226
2. Applebury M.L., Zuckerman D.M., Lamola A.A., and Jovin T.M. Rhodopsin. Purification and recombination with phospholipids assayed by the metarhodopsin I leads to metarhodopsin II transition. Biochemistry 13 (1974) 3448-3458
3. Albert A.D., and Litman B.J. Independent structural domains in the membrane protein bovine rhodopsin. Biochemistry 17 (1978) 3893-3900
4. Anderson R.E., Landis D.J., and Dudley P.A. Essential fatty acid deficiency and renewal of rod outer segments in the albino rat. Inv. Ophthal. 15 (1976) 232-236
5. Amis S., and Hofmann K.P. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl. Acad. Sci. USA 90 (1993) 7849-7853
6. Aton B., and Litman B.J. Activation of rod outer segment phosphodiesterase by enzymatically altered rhodopsin: a regulatory role for the carboxyl terminus of rhodopsin. Exp. Eye Res. 38 (1984) 547-559
7. Attwood P.V., and Guffreund H. The application of pressure relaxation to the study of the equilibrium metarhodopsin I and II from bovine retinas. FEBS Lett. 119 (1980) 323-326
8. Baldwin J. The probable arrangement of the helices in G protein-coupled receptors. EMBO J.I 4 (1993) 1693-1703
9. Baldwin P.A., and Hubbell W.L. Effects of lipid environment on the light-induced conforma-tional changes of rhodopsin 1. Absence of metarhodopsin II production indimyristoylphospha-tidylcholine recombinant membranes. Biochemistry 24 (1985) 2624-2632
10. Baldwin P.A., and Hubbell W.L. Effects of lipid environment on the light-induced conforma-tional changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state. Biochemistry 24 (1985) 2633-2639
11. Barclay P.L., and Findlay J.B. Labelling of the cytoplasmic domains of bovine rhodopsin with hydrophilic chemical probes. Biochem. J. 220 (1984) 75-84
12. Bennett N., Michel-Villaz M., and Kuhn H. Light-induced interaction between rhodopsin and the GTP-binding protein. Metarhodopsin II is the major photoproduct involved. E. J. Biochem. 127 (1982) 97-103
13. Birge R.R., Einterz C.M., Knapp H.M., and Murray L.P. The nature of the primary photochemical events in rhodopsin and isorhodopsin. Biophys. J. 53 (1988) 367-385
14. Blatz P.E., Mohler J.H., and Navangul H.V. Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal. Biochemistry 11 (1972) 848-855
15. Blazynski C., and Ostroy S.E. Pathways in the hydrolysis of vertebrate rhodopsin. Vis. Res. 24 (1984) 459-470
16. Boucher F., and Leblanc R.M. Energy storage in the primary photoreaction of bovine rhodopsin. A photoacoustic study. Photochem. Photobiol. 41 (1985) 459-465
17. Bownds D. Site of attachment of retinal in rhodopsin. Nature 216 (1967) 1178-1181
18. Chabre M., and 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. Vis. Res. 19 (1979) 1005-1018
19. Cone R.A. Rotational diffusion of rhodopsin in the visual receptor membrane. Nature New Biol. 236 (1972) 39-43
20. Cooper A. Energy uptake in the first step of visual excitation. Nature 282, 531-533. Dartnall, H. J. A. 1968 . The photosensitivities of visual pigmentsin the presence of hydroxylamine. Vis. Res. 8 (1979) 339-358
21. Davidson F.F., Loewen P.C., and Khorana H.G. Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin,affects the light-activated metarhodopsin II state. Proc. Natl. Acad. Sci. USA 91 (1994) 4029-4033
22. DeGrip W.J., Gillespie J., and Rothschild K.J. Carboxyl group involvement in the meta I and meta II stages in rhodopsin bleaching. A Fourier transform infrared spectroscopic study. Biochim. Biophys. Acta 809 (1985) 97-106
23. Doi T., Molday R.S., and Khorana H.G. Role of the intradiscal domain in rhodopsin assembly and function. Proc. Natl. Acad. Sci. USA 87 (1990) 4991-4995
24. Doukas A.G., Aton B., Callender R.H., and Ebrey T.G. Resonance Raman studies of bovine metarhodopsin I and metarhodopsin II. Biochemistry 17 (1978) 2430-2435
25. Emeis D., Kuhn H., Reichert J., and Hofmann K.P. Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium. FEBS Lett. 143 (1982) 29-34
26. Fahmy K., Jager F., Beck M., Zvyaga T.A., Sakmar T.P., and Siebert F. Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-trans-form infrared spectroscopy study of site-dir. Proc. Natl. Acad. Sci. USA 90 (1993) 10206-10210
27. Falk G., and Fatt P. Rapid hydrogen ion uptake of rod outer segments and rhodopsin solutions on illumination. J. Physiol. (Lond) 183 (1966) 211-224
28. Farahbakhsh Z.T., Hideg K., and Hubbell W.L. Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 262 (1993) 1416-1419
29. Findlay J.B., Brett M., and Pappin D.J. Primary structure of C-terminal functional sites in bovine rhodopsin. Nature 293 (1981) 314-317
30. Franke R.R., Konig B., Sakmar T.P., Khorana H.G., and Hofmann K.P. Rhodopsin mutants that bind but fail to activate transducin. Science 250 (1990) 123-125
31. Franke R.R., Sakmar T.P., Graham R.M., and Khorana H.G. Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267 (1992) 14767-14774
32. Fukuda M.N., Papermaster D.S., and Hargrave P.A. Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus. J. Biol. Chem. 254 (1979) 8201-8207
33. Fung B.K., and Hubbell W.L. Organization of rhodopsin in photoreceptor membranes. 1. Proteolysis of bovine rhodopsin in native membranes and the distribution of sulfhydryl groups in the. Biochemistry 17 (1978) 4396-4402
34. Fung B.K., and Hubbell W.L. Organization of rhodopsin in photoreceptor membranes. 2. Transmembrane organization of bovine rhodopsin: evidence from proteolysis andlactoperoxi-dase-catalyzed iodination of native and reconstituted membranes. Biochemistry 17 (1978) 4403-4410
35. Ganter U.M., Charitopoulos T., Virmaux N., and Siebert F. Conformational changes of cytosolic loops of bovine rhodopsin during the transition to metarhodopsin-II: an investigation by Fourier transform infrared differ. Photochem. Photobiol. 56 (1992) 57-62
36. Garcia-Quintana D., Garriga P., and Manyosa J. Quantitative characterization of the structure of rhodopsin in disc membrane by means of Fourier transform infrared spectroscopy. J. Biol. Chem. 268 (1993) 2403-2409
37. Gibson N.J., and Brown M.F. Role of phosphatidylserine in the MI-MII equilibrium of rhodopsin. Biochem. Biophys. Res. Comm. 176 (1991) 915-921
38. Gibson N.J., and Brown M.F. Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes. Biochemistry 32 (1993) 2438-2454
39. Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA 82 (1985) 3665-3669
40. Hargrave P.A., McDowell J.H., Curtis D.R., Wang J.K., Juszczak E., Fong S.L., Rao J.K., and Argos P. The structure of bovine rhodopsin. Biophys. Struc., Mech. 9 (1983) 235-244
41. Hargrave P.A., Hamm H., and Hofmann K.P. Interaction of rhodopsin with the G-protein, transducin. Bioessays 15 (1993) 43-50
42. Henderson R., Baldwin J.M., and Ceska T.A. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 899-929
43. Hoffmann W., Siebert F., Hofmann K.P., and Kreutz W. Two distinct rhodopsin molecules within the disc membrane of vertebrate rod outer segments. Biochim. Biophys. Acta 503 (1978) 450-461
44. Hofmann K.P., Emeis D., and Schnetkamp P.P. Interplay between hydroxylamine, metarho-dopsin II and GTP-binding protein in bovine photoreceptor membranes. Biochim. Biophys. Acta 725 (1983) 60-70
45. Hubbard R., and Kropf R. The action of light on rhodopsin. Proc. Natl. Acad. Sci. USA 44 (1958) 130-139
46. Hug S.J., Lewis J.W., and Kliger D.S. Evidence for a common batho intermediate of rhodopsin and isorhodopsin. J. Am. Chem. Soc. 110 (1988) 1998-1999
47. Hug S.J., Lewis J.W., Einterz C.M., Thorgeirsson T.E., and Kliger D.S. Nanosecond photolysis of rhodopsin: evidence for a new, blue-shifted intermediate. Biochemistry 29 (1990) 1475-1485
48. Kahlert M., and Hofmann K.P. Reaction rate and collisional efficiency of the rhodopsin-transducin system in intact retinal rods. Biophys. J. 59 (1991) 375-386
49. Kandori H., Shichida Y., and Yoshizawa T. Absolute absorption spectra of batho-and photor-hodopsins at room temperature. Picosecond laser photolysis of rhodopsin in polyacrylamide. Biophys. J. 56 (1989) 453-457
50. Kariel N., Davidson E., and Keough K. Cholesterol does not remove the gel liquid crystalline phase transition of phosphatidylcholines containing two polyenoic acyl chains. Biochim. Biophys. Acta 1062 (1991) 70-76
51. Karnik S.S., Sakmar T.P., Chen H.B., and Khorana H.G. Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc. Natl. Acad. Sci. USA 85 (1988) 8459-8463
52. Karnik S.S., and Khorana H.G. Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J. Biol. Chem. 265 (1990) 17520-17524
53. Kaushal S., Ridge K.D., and Khorana H.G. Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 91 (1994) 4024-4028
54. Keough K., and Kariel N. Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chairs. Biochim. Biophys. Acta 902 (1987) 11-18
55. Khan S.M., Bolen W., Hargrave P.A., Santoro M.M., and McDowell J.H. Differential scanning calorimetry of bovine rhodopsin in rod-outer-segment disk membranes. E. J. Biochem. 200 (1991) 53-59
56. Khorana H.G. Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function. J. Biol. Chem. 267 (1992) 1-4
57. t-activating form of photolyzed bovine rhodopsin. Biochemistry 30 (1991) 6761-6768
58. Klinger A.L., and Braiman M.S. Structural comparison of metarhodopsin II, metarhodopsin III, and opsin based on kinetic analysis of Fourier transform infrared difference spectra. Biophys. J. 63 (1992) 1244-1255
59. Konig B., Arendt A., McDowell J.H., Kahlert M., Hargrave P.A., and Hofmann K.P. Three cytoplasmic loops of rhodopsin interact with transducin. Proc. Natl. Acad. Sci.USA. 86 (1989) 6878-6882
60. Kropf A. Intramolecular energy transfer in rhodopsin. Vis. Res. 7 (1967) 811-818
61. Kühn H., and Hargrave P.A. Light-induced binding of Guanosinetriphosphate to bovine photoreceptor membranes: Effect of limited proteolysis of the membranes. Biochemistry 20 (1981) 2410-2417
62. Lamola A.A., Yamane T., and Zipp A. Effects of detergents and high pressures upon the metarhodopsin I 2ar metarhodopsin II equilibrium. Biochemistry 13 (1974) 738-745
63. Lewis J.W., and Kliger D.S. Photointermediates of visual pigments. J. Bioenerg. Biomem. 24 (1992) 201-210
64. Lewis J.W., Winterte J.S., Powers M.A., Kliger D.S., and Dratz E.A. Kinetics of rhodopsin photolysis intermediates in retinal rod disk membranes. I. Temperature dependence of lumirho-dopsin and metarhodopsin I kinetics. Photochem. Photobiol. 34 (1981) 375-384
65. Lewis J.W., Hug S.J., Wallace-Williams S.E., and Kliger D.S. Direct evidence for an equilibrium between early photolysis intermediates of rhodopsin. J. Am. Chem. Soc. 112 (1990) 6711-6712
66. Liang C.J., Yamashita K., Muellenberg C.G., Shichi H., and Kobata A. Structure of the carbohydrate moieties of bovine rhodopsin. J. Biol. Chem. 254 (1979) 6414-6418
67. Liebman P.A. In situ microspectrophotometric studies on the pigments of single retinal rods. Biophys. J. 2 (1962) 161-178
68. Litman B.J., Kalisky O., and Ottolenghi M. Rhodopsin-phospholipid interactions: dependence of rate of the meta I to meta II transition on the level of associated disk phospholipid. Biochemistry 20 (1981) 631-634
69. Litman B.J., Aton B., and Hartley J.B. Functional domains of rhodopsin. Vis. Res. 22 (1982) 1439-1442
70. Litman B.J. Methods for determining rod outer segment disk phospholipid transmembrane topology. Meth. In Enzymol. 81 (1982) 309-315
71. Litman B.J., Lewis E.N., and Levin I.W. Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellarphosphatidylcholine dispersions. Biochem-istry 30 (1991) 313-319
72. In press. Litman B.J., and Mitchell D.C. A role for phospholipid polyunsaturation in modulating membrane protein function. Lipids (1996)
73. Longstaff C., Calhoon R., and Rando R. Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein. Proc. Natl. Acad. Sci. 83 (1986) 4209-4213
74. Martynov V.I., Kostina M.B., Feigina M.I., and Miroshnikov A.I. Study of the molecular organization of visual rhodopsin in photoreceptor membranes by limited proteolysis. Bioorganich. Khim. 9 (1983) 734-745
75. Mathews R., Hubbard R., Brown P., and Wald G. Tautomeric forms of metarhodopsin. J. Gen. Phys. 47 (1963) 215-240
76. Mathies R., Oseroff A.R., and Stryer L. Rapid-flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin. Proc. Natl. Acad. of Sci. USA 73 (1976) 1-5
77. McDowell J.H., Nawrocki J.P., and Hargrave P.A. Phosphorylation sites in bovine rhodopsin. Biochemistry 32 (1993) 4968-4974
78. Michel-Villaz M., Saibil H.R., and Chabre M. Orientation of rhodopsin alpha-helices in retinal rod outer segment membranes studied by infrared linear dichroism. Proc. Natl. Acad. Sci. USA 76 (1979) 4405-4408
79. Michel-Villaz M., Roche C., and Chabre M. Orientational changes of the absorbing dipole or retinal upon the conversion of rhodopsin to bathorhodopsin, lumirhodopsin, and isorhodopsin. Biophys.J. 37 (1982) 603-616
80. Miller J.L., Fox D.A., and Litman B.J. Amplification of phosphodiesterase activation is greatly reduced by rhodopsin phosphorylation. Biochemistry 25 (1986) 4983-4988
81. Mitchell D.C., Straume M., Miller J.L., and Litman B.J. Modulation of metarhodopsin formation by cholesterol-induced ordering of bilayer lipids. Biochemistry 29 (1990) 9143-9149
82. Mitchell D.C., Kibelbek J., and Litman B.J. Rhodopsin in dimyristoylphosphatidylcholine-re-constituted bilayers forms metarhodopsin II and activates Gt. Biochemistry 30 (1991) 37-42
83. Mitchell D.C., Kibelbek J., and Litman B.J. Effect of phosphorylation on receptor conforma-tion: the metarhodopsin I in equilibrium with metarhodopsin II equilibrium in multiply phospho-rylated rhodopsi. Biochemistry 31 (1992) 8107-8111
84. Mitchell D.C., Straume M., and Litman B.J. Role of sn-1-saturated, sn-2-polyunsaturated phospholipids in control of membrane receptor conformational equilibrium: effects of cholesterol and acyl chain u the metarhodopsin I in equilibrium with metarhodopsin II equilibrium. Biochemistry 31 (1992) 662-670
85. Molday R.S., and Molday L.L. Identification and characterization of multiple forms of rhodopsin and minor proteins in frog and bovine rod outer segment disc membranes. Electrophoresis,lectin labeling, and proteolysis studies. J. Biol. Chem. 254 (1979) 4653-4660
86. Mone A.P., and Litman B.J. Cholesterol increases the stability of rhodopsin in egg PC vesicles to thermally induced unfolding. Biophys. J. 57 (1990) 74a
87. Mone A.P., and Litman B.J. Variation of phospholipid headgroup composition modulates the formation of metarhodopsin II. Biophys. J. 59 (1991) 621a
88. Monger T.G., Alfano R.R., and Callender R.H. Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale. Biophys. J. 27 (1979) 105-115
89. Mouritsen O.G., and Bloom M. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46 (1984) 141-153
90. Mullen E., and Akhtar M. Topographic and active-site studies on bovine rhodopsin. FEBS Lett. 132 (1981) 261-264
91. Mullen E., and Akhtar M. Structural studies on membrane-bound bovine rhodopsin. Biochem. J. 211 (1983) 45-54
92. Nakayama T.A., and Khorana H.G. Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265 (1990) 15762-15769
93. Nakayama T.A., and Khorana H.G. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol. Chem. 266 (1991) 4269-4275
94. Nathans J., and Hogness D.S. Isolation, sequence analysis, and intro-econ arrangement of the gene encoding bovine rhodopsin. Cell 34 (1983) 807-814
95. Nathans J. Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin. Biochemistry 29 (1990) 9746-9752
96. Nathans J. Determinants of visual pigment absorbance: role of charged amino acids in the putative transmembrane segments. Biochemistry 29 (1990) 937-942
97. Nathans J. Rhodopsin: Structure function, and genetics. Biochemistry 31 (1992) 4923-4931
98. Needham D., and Nunn R.S. Elastic deformation and failure of lipid bilayer membranes containing cholesterol. Biophys. J. 58 (1990) 997-1009
99. Neuringer M., Condor W.E., Van P.C., and Barstad L. Dietary omega-3 fatty acid deficiency and visual loss in infant Rhesus monkeys. J. Clin. Invest. 73 (1984) 272-276
100. O'Brien D.F., Costa L.F., and Ott R.A. Photochemical functionality of rhodopsin-phospholipid recombinant membranes. Biochemistry 16 (1977) 1295-1303
101. Ovchinnikov Y.A., Abdulaev N.G., Feigina M.I., Artamonov I.D., and Bogachuk A.S. Visual rhodopsin. III. Complete amino acid sequence and topography in a membrane. Bioorgan. Khim. 9 (1983) 1331-1340
102. Ovchinnikov Y.A., Abdulaev N.G., and Bogachuk A.S. Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Lett. 230 (1988) 1-5
103. Papac D.I., Oatis Jr. J.E., Crouch R.K., and Knapp D.R. Mass spectrometric identification of phosphorylation sites in bleached bovine rhodopsin. Biochemistry 32 (1993) 5930-5934
104. Papermaster D.S., and Dreyer W.J. Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13 (1974) 2438-2444
105. Parkes J.H., and Liebman P.A. Temperature and pH dependence of metarhodopsin I-metarho-dopsin II kinetics and equilibrium in bovine rod disk membrane suspensions. Biochemistry 23 (1984) 5054-5061
106. Pellicone C., Nullans G., and Virmaux N. Localization of light-induced conformational changes in bovine rhodopsin. FEBS Lett. 181 (1985) 179-183
107. Peters K., Applebury M.L., and Rentzepis P.M. Primary photochemical event in vision: proton translocation. Proc. Natl. Acad. Sci. USA 74 (1977) 3119-3123
108. Pfister C., Kuhn H., and Chabre M. Interaction between photoexcited rhodopsin and peripheral enzymes in frog retinal rods. Influence on the postmetarhodopsin II decay and phosphorylation rate o. E. J. Biochem. 136 (1983) 489-499
109. Pober J.S., and Stryer L. Light dissociates enzymatically-cleaved rhodopsin into two different fragments. J. Mol. Biol. 95 (1975) 477-481
110. Poo M., and Cone R.A. Lateral diffusion of rhodopsin in the photoreceptor membrane. Nature 247 (1974) 438-441
111. Randall C.E., Lewis J.W., Hug S.J., Bjorling S.C., Eisner-Shanas I., Friedman N., Ottolengi M., Sheves M., and Kliger D.S. A New photolysis intermediate in artificial and native visual pigments. J. Am. Chem. Soc. 113 (1991) 3473-3485
112. Resek J.F., Farahbakhsh Z.T., Hubbell W.L., and Khorana H.G. Formation of the meta II photointermediate is accompanied by changes in the cytoplasmic surface of rhodopsin. Biochem-istry 32 (1993) 12025-12032
113. Robinson P.R., Cohen G.B., Zhukovsky E.A., and Oprian D.D. Constitutively active mutants of rhodopsin. Neuron 9 (1992) 719-725
114. Rohlich P. Photoreceptor membrane carbohydrate on the intradiscal surface of retinal rod disks. Nature 263 (1976) 789-791
115. Rothschild K.J., Gillespie J., and DeGrip W.J. Evidence for rhodopsin refolding during the decay of Meta II. Biophys. J. 51 (1987) 345-350
116. Sakmar T.P., Franke R.R., and Khorana H.G. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA 86 (1989) 8309-8313
117. Salem Jr. N. Omega-3 fatty acids: Molecular and biochemical aspects. In: Spiller G.A., and Scala J. (Eds). New Protective Roles for Selected Nutrients (1989), Alan R. Liss Inc., New York, NY. 109-228
118. Schertier G.F., Villa C., and Henderson R. Projection structure of rhodopsin. Nature 362 (1993) 770-772
119. Schick G.A., Cooper T.M., Holloway R.A., Murray L.P., and Birge R.R. Energy storage in the primary photochemical events of rhodopsin and isorhodopsin. Biochemistry 26 (1987) 2556-2562
120. Shichi H., and Shelton E. Assessment of physiological integrity of sonicated retinal rod membranes. J. Supramol Struct. 2 (1974) 7-16
121. Singer S.J., and Nicholson G.L. The fluid mosaic model of cell membranes. Science 175 (1972) 720-731
122. Smith Jr. H.G., Stubbs G.W., and Litman B.J. The isolation and purification of osmotically intact discs from retinal rod outer segments. Exp. Eye Res. 20 (1975) 211-217
123. Smith S.O., Courtin J., de Groot H., Gebhard R., and Lugtenburg J. 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry 30 (1991) 7409-7415
124. Stewart J.G., Baker B.N., and Williams T.P. Evidence for conformeric states of rhodopsin. Biophys. Struc. Mech. 3 (1977) 19-29
125. Stone W.L., Farnsworth C.C., and Dratz E.A. A reinvestigation of the fatty acid content of bovine. Rat and frog retinal rod outer segments. Exp. Eye Res. 28 (1979) 387-397
126. Straume M., and Litman B.J. Influence of cholesterol on equilibrium and dynamic bilayer structure of unsaturated acyl chain phosphatidylcholine vesicles as determined from higherorder analysis of fluorescence anisotropy decay. Biochemistry 26 (1987) 5121-5126
127. Straume M., and Litman B.J. Equilibrium and dynamic structure of large, unilamellar, unsaturated acyl chain phosphatidylcholine vesicles. Higher order analysis of l,6-diphenyl-l,3,5-hexa l-[4- (trimethylammonio) phenyl]-6-phenyl-l,3,5-hexatriene anisotropy decay. Biochemistry 26 (1987) 5113-5120
128. Straume M., Mitchell D.C., Miller J.L., and Litman B.J. Interconversion of metarhodopsins I and II: a branched photointermediate decay model. Biochemistry 29 (1990) 9135-9142
129. Stryer L. Visual excitation and recovery. J. Biol. Chem. 266 (1991) 10711-10714
130. Stubbs G.W., and Litman B.J. Microviscosity of the hydrocarbon region of the bovine retinal rod outer segment disk membrane determined by fluorescent probe measurements. Biochemistry 15 (1976) 2766-2772
131. Stubbs G.W., and Litman B.J. Effect of alterations in the amphipathic microenvironment on the conformational stability of bovine opsin. 1. Mechanism of solubilization of disk membranes by the nonionic detergent, octyl glucoside. Biochemistry 17 (1978) 215-219
132. Thomas D.D., and Stryer L. Transverse location of the retinal chromophore of rhodopsin in rod outer segment disc membranes. J. Mol. Biol. 154 (1982) 145-157
133. Thorgeirsson T.E., Lewis J.W., Wallace-Williams S.E., and Kliger D.S. Photolysis of rhodopsin results in deprotonation of its retinal Schiff's base prior to formation of metarhodopsin II. Photochem. Photobiol. 56 (1992) 1135-1144
134. Thorgeirsson T.E., Lewis J.W., Wallace-Williams S.E., and Kliger D.S. Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II. Biochemistry 32 (1993) 13861-13872
135. Trayhurn P., Mandel P., and Virmaux N. Removal of a large fragment of rhodopsin without changes in its spectral properties, by proteolysis of retinal rod outer segments. FEBS Lett. 38 (1974) 351-353
136. Wang J.K., McDowell J.H., and Hargrave P.A. Site of attachment of 11-cis-retinal in bovine rhodopsin. Biochemistry 19 (1980) 5111-5117
137. Weitz C.J., and Nathans J. Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II. Neuron 8 (1992) 465-472
138. Wiedmann T.S., Pates R.D., Beach J.M., Salmon A., and Brown M.F. Lipid-protein interactions mediate the photochemical function of rhodopsin. Biochemistry 27 (1988) 6469-6474
139. Wilden U., Hall S.W., and Kuhn H. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segmen. Proc. Natl. Acad. Sci. USA 83 (1986) 174-1178
140. Wong J.K., and Ostroy S.E. Hydrogen ion changes of rhodopsin I. Proton uptake during the metarhodopsin I 478 metarhodopsin II 380 reaction. Arch. Biochem. Biophys 154 (1973) 1-7
141. Yan M., Manor D., Weng G., Chao H., Rothberg L., Jedju T.M., Alfano R.R., and Callender R.H. Ultrafast spectroscopy of the visual pigment rhodopsin. Proc. Natl. Acad. Sci. USA 88 (1991) 9809-9812
142. Zhukovsky E.A., and Oprian D.D. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 246 (1989) 928-930
143. Zvyaga T.A., Min K.C., Beck M., and Sakmar T.P. Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II trans. J. Biol. Chem. 268 (1993) 4661-4667
144. Zvyaga T.A., Fahmy K., and Sakmar T.P. Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin. Biochemistry 33 (1994) 9753-9761