Direct Measurements for Isomer Ratio of Retinal in Bacteriorhodopsin by an Electrochemical Method

Photochemistry and Photobiology

Volumn 66, Issue 6, 1997, Pages 784-787

  Koyama, Koichi ^a,b  

^a HOKKAIDO UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0345847952     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1997.tb03224.x     Document Type: Article

References (27)

1. Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckman and K. H. Downing (1990). Model for the structure of bacteriorhodopsin based on high-resolution cryo-microscopy. J. Mol. Biol. 213, 899-929.
2. Brown, L. S., J. Sasaki, H. Kandori, A. Maeda, R. Needleman and J. K. Lanyi (1995) Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270, 27122-27126.
3. Trissl, H.-W. (1990) Photoelectric measurements of purple membranes. Photochem. Photobiol. 51, 793-818.
4. Hong, F. T. (1994) Retinal proteins in photovoltaic devices. In Molecular and Biomolecular Electronics, ACS advances in chemistry series no. 240 (Edited by R. R. Birge), pp. 527-559. Americal Chemical Society, Washington, DC.
5. Miyasaka, T., K. Koyama and I. Itoh (1992) Quantum conversion and image detection by a bacteriorhodopsin-based artificial photoreceptor. Science 255, 342-344.
6. Miyasaka, T. and K. Koyama (1993) Image sensing and processing by bacteriorhodopsin-based artificial photoreceptor. Appl. Opt. 32, 6371-6379.
7. Stoeckenius, W., R. H. Lozier and R. A. Bogomoloni (1979). Bacteriorhodopsin and the purple membrane of halobacteria. Biochim. Biophys. Acta 505, 215-278.
8. Oesterhelt, D., M. Meentzen and L. Schumann (1973). Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans retinal as its chromophores. Eur. J. Biochem. 40, 453-463.
9. Sperling, W., P. Carl, C. Rafferty and N. Dencher (1977) Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers. Biophys. Struct. Mech. 3, 79-94.
10. Ohno, K., Y. Takeuchi and M. Yoshida (1977) Light-induced formation of the 410 nm intermediate from reconstituted bacteriorhodopsin. J. Biochem. (Tokyo) 82, 1177-1180.
11. Maeda, A., T. Iwasa and T. Yoshizawa (1977) Isomeric composition of retinal chromophore in dark-adapted bacteriorhodopsin. J. Biochem. (Tokyo) 82, 1599-1604.
12. Pettei, M. J., A. P. Yudd, K. Nakanishi, R. Henselman and W. Stoeckenius (1977) Identification of retinal isomers isolated from bacteriorhodopsin. Biochemistry 16, 1955-1959.
13. Tsuda, M., M. Glaccum, B. Nelson and T. Ebrey (1980) Light isomerizes the chromophore of bacteriorhodopsin. Nature 287, 351-353.
14. Scherrer, P., M. K. Mathew, W. Sperling and W. Stoeckenius (1989) Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomer. Biochemistry 28, 829-834.
15. Oesterhelt, D. and W. Stoeckenius (1974) Isolation of the cell membrane of Halobacterium halobium and its fraction into red and purple membrane. Methods Enzymol. 31, 667-678.
16. Miyasaka, T. and K. Koyama (1992) Rectified photocurrents from purple membrane Langmuir-Blodgett films at the electrode-electrolyte interface. Thin Solid Film 210/211, 146-149.
17. Yamaguchi, N., Y. Jinbo, Y. Arai and K. Koyama (1993) Visualization of morphology of purple membrane surfaces by monoclonal antibody techniques. FEBS Lett. 324, 287-292.
18. Koyama, K., N. Yamaguchi and T. Miyasaka (1994) Antibody-mediated bacteriorhodopsin orientation for molecular device architectures. Science 265, 762-765.
19. Váró, G. and K. Bryl (1988) Light-and dark-adaptation of bacteriorhodopsin measured by a photoelectric method. Biochim. Biophys. Acta 934, 247-252.
20. Smith, S., H. De Groot, R. Gebhard, M. Courtin, J. Lugtenburg, J. Herzfeld and R. Griffin (1989) Structure and protein environment of the retinal chromophore in light-and dark-adapted bacteriorhodopsin studied by solid-state NMR. Biochemistry 28, 8897-8904.
21. Eisenstein, L., S. Lin, G. Dollinger, K. Odashima, J. Termini, K. Konno, N. Ding and K. Nakanishi (1987) FTIR difference studies on apoproteins. Protonation states of aspartic and glutamic acid residues during the photocycle of bacteriorhodopsin. J. Am. Chem. Soc. 109, 6860-6862.
22. Ames, J. B., S. R. Bolton, M. M. Netto and R. A. Mathies (1990) Ultraviolet resonance raman spectroscopy of bacteriorhodopsin: evidence against tyrosinate in the photocycle. J. Am. Chem. Soc. 112, 9007-9009.
23. Ohno, K., Y. Takeuchi and M. Yoshida (1977) Effect of light-adaptation on the photoreaction of bacteriorhodopsin from Halobacterium halobium. Biochim. Biophys. Acta 462, 575-582.
24. Robertson, B. and E. P. Lukashev (1995) Rapid pH change due to bacteriorhodopsin measured with a tin-oxide electrode. Biophys. J. 68, 1507-1517.
25. Balashov, S. P., E. S. Imasheva, R. Govindjee and T. G. Ebrey (1996) Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70, 473-481.
26. Balashov, S. P., R. Govindjee, M. Kono, E. S. Imasheva, E. Lukashev, T. G. Ebrey, R. K. Crouch, D. R. Menick and Y. Feng (1993) Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle. Biochemistry 32, 10331-10343.
27. Balashov, S. P., R. Govindjee, E. S. Imasheva, S. Misra, T. G. Ebrey, R. K. Crouch and D. R. Menick (1995) The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin. Biochemistry 34, 8820-8834.