Photoelectrochemical Verification of Proton-Releasing Groups in Bacteriorhodopsin

Photochemistry and Photobiology

Volumn 68, Issue 3, 1998, Pages 400-406

  Koyama, Koichi ^a,b   Miyasaka, Tsutomu ^b   Needleman, Richard ^c   Lanyi, Janos K ^d  

^a HOKKAIDO UNIVERSITY   (Japan)

^b FUJIFILM CORPORATION   (Japan)

^c WAYNE STATE UNIVERSITY   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUS;

EID: 0001559623     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1998.tb09699.x     Document Type: Article

References (47)

1. Lanyi, J. K. (1993) Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta 1183, 241-261.
2. Krebs, M. P. and H. G. Khorana (1993) Mechanism of light-dependent proton translocation by bacteriorhodopsin. J. Bacteriol. 175, 1555-1560.
3. Bousché, O., S. Sonar, M. P. Krebs, H. G. Khorana and K. J. Rothschild (1992) Time-resolved FTIR spectroscopy of the bacteriorhdopsin mutant Try 185 → Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay. Photochem. Photobiol. 56, 1085-1095.
4. Zimányi, L., G. Váró, M. Chang, B. Ni, R. Needleman and J. K. Lanyi (1992) Pathway of proton release in the bacteriorhodopsin photocycle. Biochemistry 31, 8535-8543.
5. 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.
6. Richter, H. T., L. S. Brown, R. Needleman and J. K. Lanyi (1996) A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry 35, 4054-4062.
7. 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.
8. Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick and R. K. Crouch (1997) Glutamate-194 to cystein mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry 36, 8671-8676.
9. Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saito, Y. Kimura, R. Needleman and J. K. Lanyi (1998) Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry 37, 2496-2506.
10. Cao, Y., G. Váró, A. L. Klinger, D. M. Czajkowsky, M. S. Braiman, R. Needleman and J. K. Lanyi (1993) Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change. Biochemistry 32, 1981-1990.
11. Govindjee, R., S. Misra, S. P. Balashov, T. G. Ebrey, R. K. Crouch and D. R. Menick (1996) Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin. Biophys. J. 71, 1011-1023.
12. Trissl, H.-W. (1990) Photoelectric measurements of purple membranes. Photochem. Photobiol. 51, 793-818.
13. Hong, F. (1994) Photovoltaic effects in biomembranes. IEEE Eng. Med. Biol. 13, 75-93.
14. Fahr, A., P. Lauger and E. Bamberg (1981) Photocurrent kinetics of purple membrane sheets bound to planar bilayer membranes. J. Membr. Biol. 60, 51-62.
15. Liu, S. Y. (1990) Light-induced currents from oriented purple membrane: I. Correlation of the microsecond component (B2) with the L-M photocycle transition. Biophys. J. 57, 943-950.
16. Tittor, J., U. Schweiger, D. Oesterhelt and E. Bamberg (1994) Inversion of proton translocation in bacteriorhodopsin mutants D85N, D95T, and D85,96N. Biophys. J. 67, 1682-1690.
17. Moltke, S., M. P. Krebs, R. Mollaaghababa, H. G. Khorana and M. P. Heyn (1995) Intramolecular charge transfer in the bacteriorhdopsin mutants Asp85→ Asn and Asp212→ Asn: effect of pH and anions. Biophys. J. 56, 1085-1095.
18. Váró, G. and L. Keszthelyi (1983) Photoelectric signals from dried oriented purple membranes of Halobacterium halobium. Biophys. J. 43, 47-51.
19. Haronian, D. and A. Lewis (1991) Elements of a unique bacteriorhodopsin neural network architecture. Appl. Opt. 30, 597-608.
20. Miyasaka, T., K. Koyama and I. Itoh (1992) Quantum conversion and image detection by a bacteriorhodopsin-based artificial photoreceptor. Science 255, 342-344.
21. Miyasaka, T. and K. Koyama (1993) Image sensing and processing by bacteriorhodopsin-based artificial photoreceptor. Appl. Opt. 32, 6371-6379.
22. Robertson, B. and E. P. Lukashev (1995) Rapid pH change due to bacteriorhodopsin measured with a tin-oxide electrode. Biophys. J. 68, 1507-1517.
23. Ni, B., M. Chang, J. K. Lanyi and R. Needleman (1990) An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene 90, 169-172.
24. Needleman, R., M. Chang, B. Ni, G. Váró, J. Fornés, S. H. White and J. K. Lanyi (1991) Properties of Asp-212 → Asn bacteriorhodopsin suggest that Asp-212 and Asp-85 both participate in a counterion and proton acceptor complex near the Schiff base. J. Biol. Chem. 266, 11478-11484.
25. 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.
26. Yamaguchi, N., Y. Jinbo, M. Arai and K. Koyama (1993) Visualization of morphology of purple membrane surfaces by monoclonal antibody techniques. FEBS Lett. 324, 287-292.
27. Koyama, K., N. Yamaguchi and T. Miyasaka (1994) Antibody-mediated bacteriorhodopsin orientation for molecular device architectures. Science 265, 762-765.
28. 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.
29. Koyama, K. (1997) Direct measurements for isomer ratio of retinal in bacteriorhodopsin by an electrochemical method. Photochem. Photobiol. 66, 784-787.
30. Váró, G. and K. Bryl (1988) Light- and dark-adaptation of bacteriorhodopsin measured by a photoelectric method. Biochim. Biophys. Acta 934, 247-252.
31. Maeda, A., T. Iwasa and T. Yoshizawa (1977) Isomeric composition of retinal chromophore in dark-adapted bacteriorhodopsin. J. Biochem. (Tokyo) 82, 1599-1604.
32. 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.
33. 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.
34. Fahr, A. and E. Bamberg (1982) Photocurrents of dark-adapted bacteriorhodopsin on black lipid membrane. FEBS Lett. 140, 251-253.
35. Alexiev, U., R. Mollaaghababa, P. Scherrer, H. G. Khorana and M. P. Heyn (1995) Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk. Proc. Natl. Acad. Sci. USA 92, 372-376.
36. Wang, J.-P., L. Song, S.-K. Yoo and M. A. El-Sayed (1997) A comparison of the photoelectric current response resulting from the proton pumping process of bacteriorhodopsin under pulsed and CW laser excitations. J. Phys. Chem. 101, 10599-10604.
37. Tittor, J., C. Christa, D. Oesterhelt, H. J. Butt and E. Bamberg (1989) A defective proton pump, point-mutated bacteriorhodopsin Asp96→ Asn is fully reactivated azide. EMBO J. 8, 3477-3482.
38. Miller, R. and D. Oesterhelt (1990) Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor. Biochim. Biophys. Acta 1020, 57-64.
39. Kataoka, M., H. Kamikubo, F. Tokunaga, L. S. Brown, Y. Yamazaki, A. Maeda, M. Sheves, R. Needleman and J. K. Lanyi (1994) Energy coupling in an ion pump. J. Mol. Biol. 243, 621-638.
40. Grigorieff, N., T. A. Ceska, K. H. Downing, J. M. Baldwin and R. Henderson (1996) Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
41. Kimura, Y., D. G. Vassylyev, A. Miyazawa, M. Kidera, A. Matsushima, K. Mitsuoka, K. Murata, T. Hirai and Y. Fujiyoshi (1997) Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature 389, 206-211.
42. Kimura, Y., D. G. Vassylyev, A. Miyazawa, M. Kidera, A. Matsushima, K. Mitsuoka, K. Murata, T. Hirai and Y. Fujiyoshi (1997) High resolution structure of bacteriorhodopsin determined by electron crystallography. Photochem. Photobiol. 66, 764-767.
43. 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.
44. 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.
45. Kono, M., S. Misra and T. G. Ebrey (1993) pH dependence of light-induced proton release by bacteriorhodopsin. FEBS Lett. 331, 31-34.
46. Ormos, P., S. Hristova and L. Keszthelyi (1985) The effect of pH on proton transport by bacteriorhodopsin. Biochim. Biophys. Acta 809, 181-186.
47. Nachliel, E., M. Gutman, S. Kiryati, and N. A. Dencher (1996) Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane. Proc. Natl. Acad. Sci. USA 93, 10747-10752.