Spectroscopic analysis of the effect of chloride on the active intermediates of the primate L group cone visual pigment

Biochemistry

Volumn 51, Issue 50, 2012, Pages 10017-10023

  Morizumi, Takefumi ^a,b   Sato, Keita ^a   Shichida, Yoshinori ^a  

^a KYOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION MAXIMA; ACTIVE STATE; AMINO ACID RESIDUES; CHLORIDE BINDING; DECAY RATE; FOUR-GROUP; GAIN INSIGHT; PROTEIN MOIETY; RED SHIFT; RED-SHIFTED; SECOND GROUP; VISUAL PIGMENTS; WILD TYPES;

AMINO ACIDS; COLOR VISION; DECAY (ORGANIC); DOPPLER EFFECT; SPECTROSCOPIC ANALYSIS;

CHLORINE COMPOUNDS;

CHLORIDE; HISTIDINE; L GROUP CONE VISUAL PIGMENT; UNCLASSIFIED DRUG; VISUAL PIGMENT;

ARTICLE; CHEMICAL BINDING; PRIORITY JOURNAL; RED LIGHT;

ANIMALS; CHLORIDES; HEK293 CELLS; HISTIDINE; HUMANS; MACACA FASCICULARIS; MUTAGENESIS, SITE-DIRECTED; RETINAL PIGMENTS; RETINALDEHYDE; RHODOPSIN; SPECTROPHOTOMETRY;

PRIMATES;

EID: 84871300294     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300995s     Document Type: Article

References (33)

1. Hofmann, K. P., Scheerer, P., Hildebrand, P. W., Choe, H. W., Park, J. H., Heck, M., and Ernst, O. P. (2009) A G protein-coupled receptor at work: The rhodopsin model Trends Biochem. Sci. 34, 540-552
2. Shichida, Y. and Imai, H. (1998) Visual pigment: G-protein-coupled receptor for light signals Cell. Mol. Life Sci. 54, 1299-1315
3. Yokoyama, S. (2008) Evolution of dim-light and color vision pigments Annu. Rev. Genomics Hum. Genet. 9, 259-282
4. Okano, T., Kojima, D., Fukada, Y., Shichida, Y., and Yoshizawa, T. (1992) Primary structures of chicken cone visual pigments: Vertebrate rhodopsins have evolved out of cone visual pigments Proc. Natl. Acad. Sci. U.S.A. 89, 5932-5936
5. Imai, H., Kuwayama, S., Onishi, A., Morizumi, T., Chisaka, O., and Shichida, Y. (2005) Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ Photochem. Photobiol. Sci. 4, 667-674
6. Shichida, Y. and Matsuyama, T. (2009) Evolution of opsins and phototransduction Philos. Trans. R. Soc. London, Ser. B 364, 2881-2895
7. Sato, K., Yamashita, T., Imamoto, Y., and Shichida, Y. (2012) Comparative studies on the late bleaching processes of four kinds of cone visual pigments and rod visual pigment Biochemistry 51, 4300-4308
8. Crescitelli, F. (1977) Ionochromic behavior of Grecko visual pigments Science 195, 187-188
9. Fager, L. Y. and Fager, R. S. (1979) Halide control of color of the chicken cone pigment iodopsin Exp. Eye Res. 29, 401-408
10. Shichida, Y., Kato, T., Sasayama, S., Fukada, Y., and Yoshizawa, T. (1990) Effects of chloride on chicken iodopsin and the chromophore transfer reactions from iodopsin to scotopsin and B-photopsin Biochemistry 29, 5843-5848
11. --binding site in the human red and green color vision pigments Biochemistry 32, 2125-2130
12. Chou, P. Y. and Fasman, G. D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence Adv. Enzymol. Relat. Areas Mol. Biol. 47, 45-148
13. Nathans, J. (1990) Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin Biochemistry 29, 9746-9752
14. Onishi, A., Koike, S., Ida, M., Imai, H., Shichida, Y., Takenaka, O., Hanazawa, A., Komatsu, H., Mikami, A., Goto, S., Suryobroto, B., Kitahara, K., and Yamamori, T. (1999) Dichromatism in macaque monkeys Nature 402, 139-140
15. Oprian, D. D., Asenjo, A. B., Lee, N., and Pelletier, S. L. (1991) Design, chemical synthesis, and expression of genes for the three human color vision pigments Biochemistry 30, 11367-11372
16. Imai, H., Kojima, D., Oura, T., Tachibanaki, S., Terakita, A., and Shichida, Y. (1997) Single amino acid residue as a functional determinant of rod and cone visual pigments Proc. Natl. Acad. Sci. U.S.A. 94, 2322-2326
17. Kayada, S., Hisatomi, O., and Tokunaga, F. (1995) Cloning and expression of frog rhodopsin cDNA Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol 110, 599-604
18. Nagata, T., Terakita, A., Kandori, H., Kojima, D., Shichida, Y., and Maeda, A. (1997) Water and peptide backbone structure in the active center of bovine rhodopsin Biochemistry 36, 6164-6170
19. Morizumi, T., Imai, H., and Shichida, Y. (2005) Direct observation of the complex formation of GDP-bound transducin with the rhodopsin intermediate having a visible absorption maximum in rod outer segment membranes Biochemistry 44, 9936-9943
20. Hug, S. J., Lewis, J. W., Einterz, C. M., Thorgeirsson, T. E., and Kliger, D. S. (1990) Nanosecond photolysis of rhodopsin: Evidence for a new, blue-shifted intermediate Biochemistry 29, 1475-1485
21. Nakai, K., Kidera, A., and Kanehisa, M. (1988) Cluster analysis of amino acid indices for prediction of protein structure and function Protein Eng. 2, 93-100
22. Radzicka, A. and Wolfenden, R. (1988) Comparing the Polarities of the Amino Acids: Side-Chain Distribution Coefficients between the Vapor Phase, Cyclohexane, 1-Octanol, and Neutral Aqueous Solution Biochemistry 27, 1664-1670
23. Hirano, T., Imai, H., and Shichida, Y. (2003) Effect of anion binding on the thermal reverse reaction of bathoiodopsin: Anion stabilizes two forms of iodopsin Biochemistry 42, 12700-12707
24. Sun, H., Macke, J. P., and Nathans, J. (1997) Mechanisms of spectral tuning in the mouse green cone pigment Proc. Natl. Acad. Sci. U.S.A. 94, 8860-8865
25. Davies, W. I., Wilkie, S. E., Cowing, J. A., Hankins, M. W., and Hunt, D. M. (2012) Anion sensitivity and spectral tuning of middle- and long-wavelength-sensitive (MWS/LWS) visual pigments Cell. Mol. Life Sci. 69, 2455-2464
26. Tachibanaki, S., Imamoto, Y., Imai, H., and Shichida, Y. (1995) Effect of chloride on the thermal reverse reaction of intermediates of iodopsin Biochemistry 34, 13170-13175
27. Minor, D. L., Jr. and Kim, P. S. (1994) Measurement of the β-sheet-forming propensities of amino acids Nature 367, 660-663
28. Minor, D. L., Jr. and Kim, P. S. (1994) Context is a major determinant of β-sheet propensity Nature 371, 264-267
29. Okada, T. (2004) X-ray crystallographic studies for ligand-protein interaction changes in rhodopsin Biochem. Soc. Trans. 32, 738-741
30. Choe, H. W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauss, N., Hofmann, K. P., Scheerer, P., and Ernst, O. P. (2011) Crystal structure of metarhodopsin II Nature 471, 651-655
31. Ruprecht, J. J., Mielke, T., Vogel, R., Villa, C., and Schertler, G. F. (2004) Electron crystallography reveals the structure of metarhodopsin I EMBO J. 23, 3609-3620
32. Yan, E. C. Y., Kazmi, M. A., De, S., Chang, B. S. W., Seibert, C., Marin, E. P., Mathies, R. A., and Sakmar, T. P. (2002) Function of Extracellular Loop 2 in Rhodopsin: Glutamic Acid 181 Modulates Stability and Absorption Wavelength of Metarhodopsin II Biochemistry 41, 3620-3627
33. Terakita, A., Koyanagi, M., Tsukamoto, H., Yamashita, T., Miyata, T., and Shichida, Y. (2004) Counterion displacement in the molecular evolution of the rhodopsin family Nat. Struct. Mol. Biol. 11, 284-289