FTIR studies of the photoactivation processes in squid retinochrome

Biochemistry

Volumn 44, Issue 22, 2005, Pages 7988-7997

  Furutani, Yuji ^a,b,c   Terakita, Akihisa ^b,c   Shichida, Yoshinori ^b,c   Kandori, Hideki ^a,c  

^a NAGOYA INSTITUTE OF TECHNOLOGY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOPHORES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; HYDROLYSIS; ORGANIC SOLVENTS; STRUCTURE (COMPOSITION); VISION;

DEPROTONATION; PHOTOISOMERASE; RETINOCHROME; RHODOPSIN;

ENZYMES;

BACTERIORHODOPSIN; CIS ACTING ELEMENT; ISOMERASE; LIPOSOME; RETINOCHROME; RHODOPSIN; SCHIFF BASE; TRANS ACTING FACTOR; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CHROMATOPHORE; HYDROGEN BOND; HYDROLYSIS; INFRARED SPECTROSCOPY; LOW TEMPERATURE; NONHUMAN; PHOTOACTIVATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTON TRANSPORT; SQUID; TEMPERATURE; THERMOSTABILITY; VIBRATION;

ANIMALS; CARBOXYLIC ACIDS; CELL LINE; DECAPODIFORMES; HUMANS; HYDROGEN BONDING; LIGHT; PHOTOCHEMISTRY; PROTEIN STRUCTURE, SECONDARY; PROTONS; RETINAL PIGMENTS; RETINALDEHYDE; SCHIFF BASES; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

BOVINAE; CEPHALOPODA; INVERTEBRATA;

EID: 20144382486     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050219w     Document Type: Article

References (47)

1. Hara, T., and Hara, R. (1965) New photosensitive pigment found in the retina of the squid Ommastrephes, Nature 206, 1331-1334.
2. Hara, T., and Hara, R. (1967) Rhodopsin and retinochrome in the squid retina, Nature 214, 573-575.
3. Hara-Nishimura, I., Kondo, M., Nishimura, M., Hara, R., and Hara, T. (1993) Amino acid sequence surrounding the retinal-binding site in retinochrome of the squid, Todarodes pacificiis, FEBS Lett. 335, 94-98.
4. Sekiya, N., Kishigami, A., Naoki, H., Chang, C. W., Yoshihara, K., Hara, R., Hara, T., and Tokunaga, F. (1991) Fourier transform infrared spectroscopic study on retinochrome and its primary photoproduct, lumiretinochrome, FEBS Lett. 280, 107-111.
5. Hara, T., and Hara, R. (1973) Isomerization of retinal catalysed by retinochrome in the light, Nat. New Biol. 242, 39-43.
6. Hara, T., and Hara, R. (1968) Regeneration of squid retinochrome, Nature 219, 450-454.
7. Ozaki, K., Terakita, A., Hara, R., and Hara, T. (1987) Isolation and characterization of a retinal-binding protein from the squid retina, Vision Res. 27, 1057-1070.
8. Terakita, A., Hara, R., and Hara, T. (1989) Retinal-binding protein as a shuttle for retinal in the rhodopsin-retinochrome system of the squid visual cells, Vision Res. 29, 639-652.
9. Hara-Nishimura, I., Matsumoto, T., Mori, H., Nishimura, M., Hara, R., and Hara, T. (1990) Cloning and nucleotide sequence of cDNA for retinochrome, retinal photoisomerase from the squid retina, FEES Lett. 271, 106-110.
10. Nathans, J. (1990) Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin, Biochemistry 29, 9746-9752.
11. Sakmar, T. P., Franke, R. R., and Khorana, H. G. (1989) Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 86, 8309-8313.
12. Zhukovsky, E. A., and Oprian, D. D. (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments, Science 246, 928-930.
13. Terakita, A., Yamashita, T., and Shichida, Y. (2000) Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family, Proc. Natl. Acad. Sci. U.S.A. 97, 14263-14267.
14. Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Le Trong, I., Teller, D. C., Okada, T., Stenkamp, R. E., Yamamoto, M., and Miyano, M. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor, Science 289, 739-745.
15. 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.
16. Tokunaga, F., Watanabe, T., Uematsu, J., Hara, R., and Hara, T. (1990) Photoreactions of retinochrome at very low temperatures, FEBS Lett. 262, 266-268.
17. Hara, R., Hara, T., Tokunaga, F., and Yoshizawa, T. (1981) Photochemistry of retinochrome. Photochem. Photobiol. 33, 883-891.
18. Maeda, A., Ohkita, Y. J., Sasaki, J., Shichida, Y., and Yoshizawa, T. (1993) Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy, Biochemistry 32, 12033-12038.
19. Nishimura, S., Kandori, H., Nakagawa, M., Tsuda, M., and Maeda, A. (1997) Structural dynamics of water and the peptide backbone around the Schiff base associated with the light-activated process of octopus rhodopsin, Biochemistry 36, 864-870.
20. 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.
21. Furutani, Y., Shichida, Y., and Kandori, H. (2003) Structural changes of water molecules during the photoactivation processes in bovine rhodopsin, Biochemistry 42, 9619-9625.
22. Aton, B., Doukas, A. G., Callender, R. H., Becher, B., and Ebrey, T. G. (1977) Resonance Raman studies of the purple membrane, Biochemistry 16, 2995-2999.
23. Eyring, G., Curry, B., Broek, A., Lugtenburg, J., and Mathies, R. (1982) Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsin, Biochemistry 21, 384-393.
24. Baasov, T., Friedman, N., and Sheves, M. (1987) Factors affecting the C=N stretching in protonated retinal Schiff base: A model study for bacteriorhodopsin and visual pigments, Biochemistry 26, 3210-3217.
25. Kandori, H., Kinoshita, N., Shichida, Y., and Maeda, A. (1998) Protein Structural Changes in Bacteriorhodopsin upon Photoisomerization As Revealed by Polarized FTIR Spectroscopy, J. Phys. Chem. B 102, 7899-7905.
26. Kandori, H., and Shichida, Y. (2000) Direct Observation of the Bridged Water Stretching Vibrations Inside a Protein, J. Am. Chem. Soc. 122, 11745-11746.
27. Shibata, M., Tanimoto, T., and Kandori, H. (2003) Water Molecules in the Schiff Base Region of Bacteriorhodopsin, J. Am. Chem. Soc. 125, 13312-13313.
28. Tanimoto, T., Furutani, Y., and Kandori, H. (2003) Structural changes of water in the Schiff base region of bacteriorhodopsin: Proposal of a hydration switch model, Biochemistry 42, 2300-2306.
29. Kandori, H., Belenky, M., and Herzfeld, J. (2002) Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization, Biochemistry 41, 6026-6031.
30. Shimono, K., Furutani, Y., Kamo, N., and Kandori, H. (2003) Vibrational modes of the protonated Schiff base in pharaonis phoborhodopsin, Biochemistry 41, 7801-7806.
31. Jager, F., Fahmy, K., Sakmar, T. P., and Siebert, F. (1994) Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin, Biochemistry 33, 10878-10882.
32. Ozaki, K., Hara, R., and Hara, T. (1982) Dependency of absorption characteristics of retinochrome on pH and salts, Exp. Eye Res. 34, 499-508.
33. --binding site in the human red and green color vision pigments. Biochemistry 32, 2125-2130.
34. 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.
35. Knowles, A. (1980) The chloride effect in chicken red cone receptors, Vision Res. 20, 475-483.
36. Fager, L. Y., and Fager, R. S. (1979) Halide control of color of the chicken cone pigment iodopsin, Exp. Eye Res. 29, 401-408.
37. 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin, Biochemistry 24, 6955-6962.
38. 13C NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin. Evidence for a 6-S-cis conformation with negative-charge perturbation near C-12, Eur. J. Biochem. 163, 9-14.
39. Furutani, Y., Bezerra, A. G., Jr., Waschuk, S., Sumii, M., Brown, L. S., and Kandori, H. (2004) FTIR Spectroscopy of the K Photointermediate of Neurospora Rhodopsin: Structural Changes of the Retinal, Protein, and Water Molecules after Photoisomerization, Biochemistry 43, 9636-9646.
40. Palings, I., van den Berg, E. M., Lugtenburg, J., and Mathies, R. A. (1989) Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: Chromophore structure and energy storage in the primary photoproduct of vision, Biochemistry 28, 1498-1507.
41. Smith, S. O., Myers, A. B., Mathies, R. A., Pardoen, J. A., Winkel, C., van den Berg, E. M., and Lugtenburg, J. (1985) Vibrational analysis of the all-trans retinal protonated Schiff base, Biophys. J. 47, 653-664.
42. Kandori, H., Shimono, K., Sudo, Y., Iwamoto, M., Shichida, Y., and Kamo, N. (2001) Structural changes of pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: Infrared spectral comparison with bacteriorhodopsin, Biochemistry 40, 9238-9246.
43. Furutani, Y., Iwamoto, M., Shimono, K., Kamo, N., and Kandori, H. (2002) FTIR spectroscopy of the M photointermediate in pharaonis rhoborhodopsin, Biophys. J. 83, 3482-3489.
44. Mathies, R., Freedman, T. B., and Stryer, L. (1977) Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin, J. Mol. Biol. 109, 367-372.
45. Palings, I., Pardoen, J. A., van den Berg, E., Winkel, C., Lugtenburg, J., and Mathies, R. A. (1987) Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for chromophore structure and environment, Biochemistry 26, 2544-2556.
46. Kandori, H., Kinoshita, N., Yamazaki, Y., Maeda, A., Shichida, Y., Needleman, R., Lanyi, J. K., Bizounok, M., Herzfeld, J., Raap, J., and Lugtenburg, J. (1999) Structural change of threonine 89 upon photoisomerization in bacteriorhodopsin as revealed by polarized FTIR spectroscopy, Biochemistry 38, 9676-9683.
47. Kandori, H., Yamazaki, Y., Shichida, Y., Raap, J., Lugtenburg, J., Belenky, M., and Herzfeld, J. (2001) Tight Asp-85-Thr-89 association during the pump switch of bacteriorhodopsin, Proc. Natl. Acad. Sci. U.S.A. 98, 1571-1576.