Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13- cisbacteriorhodopsin

Biophysical Journal

Volumn 71, Issue 4, 1996, Pages 1973-1984

  Balashov, Sergei P ^a,b   Imasheva, Eleonora S ^a,b   Govindjee, Rajni ^a   Sheves, Mordechai ^c   Ebrey, Thomas G ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

13 BACTERIORHODOPSIN; ASPARTIC ACID; BACTERIORHODOPSIN; PROTON PUMP; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; CELL TRANSFORMATION; CHEMICAL REACTION KINETICS; LIGHT ADAPTATION; MATHEMATICAL MODEL; MEMBRANE STRUCTURE; PKA;

BACTERIA (MICROORGANISMS);

EID: 0029845351     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79395-5     Document Type: Article

References (60)

1. a'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.
2. Balashov, S. P., R. Govindjee, M. Kono, E. 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.
3. Balashov, S. P., E. S. Imasheva, R. Govindjee, and T. G. Ebrey. 1991. Quantum yield ratio of the forward and back light reactions of bacteriorhodopsin at low temperature and photosteady-state concentration of the bathoproduct K. Photochem. Photobiol. 54:955-961.
4. 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.
5. Balashov, S. P., F. F. Litvin, and V. A. Sineshchekov. 1988. Photochemical processes of light energy transformation in bacteriorhodopsin. Sov. Sci. Rev. Sect. D. Physicochem. Biol Rev. 8:1-61.
6. Becher, B., and J. Y. Cassim. 1975. Improved isolation procedures for the purple membrane of Halobacterium halobium. Prep. Biochem. 5:161-178.
7. Birge, R. R. 1990. Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta. 1016:293-327.
8. a increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins. Biophys. J. 70:939-947.
9. 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.
10. Chang, C-H., J.-G. Chen, R. Govindjee, and T. G. Ebrey. 1985. Cation binding by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 82:396-400.
11. Chang, C. H., S. Y. Liu, R. Jonas, and R. Govindjee. 1987. The pink membrane: the stable photoproduct of deionized purple membrane. Biophys. J. 52:617-623.
12. 15N NMR study of the low pH forms of bacteriorhodopsin. Biochemistry. 29:6873-6883.
13. Dunach, M., T. Marti, H. G. Khorana, and K. J. Rothschild. 1990. UV-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation. Proc. Natl. Acad. Sci. USA. 87:9873-9877.
14. Ebrey, T. G. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membrane Receptors and Channels. M. B. Jackson, editor. CRC Press, Boca Raton. 353-378.
15. Fischer, U., and D. Oesterhelt. 1979. Chromophore equilibria in bacteriorhodopsin. Biophys. J. 28:211-230.
16. Fischer, U. Ch., P. Towner, and D. Oesterhelt. 1981. Light-induced isomerization, at acidic pH, initiates hydrolysis of bacteriorhodopsin to bacterio-opsin and 9-cis-retinal. Photochem. Photobiol. 33:529-537.
17. Fodor, S. P. A., J. B. Ames, R. Gebhard, E. M. M. van den Berg, W. Stoeckenius, J. Lugtenburg, and R. A. Mathies. 1988. Chromophore structure in bacteriorhodopsins's N intermediate: implications for the proton-pumping mechanism. Biochemistry. 27:7097-7101.
18. a of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem. Soc. 115:3772-3773.
19. Harbison, G. S., S. O. Smith, J. A. Pardoen, C. Winkel, J. Lugtenberg, J. Herzfeld, R. Mathies, and R. G. Griffin. 1984. Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff base. Proc. Nail. Acad. Sci. USA. 81:1706-1709.
20. He, Y., M. P. Krebs, W. B. Fischer, H. G. Khorana, and K. J. Rothschild. 1993. FTIR difference spectroscopy of the bacteriorhodopsin mutant Tyr-185-> Phe: detection of a stable O-like species and characterization of its photocycle at low temperature. Biochemistry. 32:2282-2290.
21. Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 899-929.
22. Ihara K., T. Amemiya, Y. Miyashita, and Y. Mukohata. 1994. Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs. Biophys. J. 67:1187-1191.
23. Jonas, R., and T. G. Ebrey. 1991. Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin. Proc. Nail. Acad. Sci. USA. 88:149-153.
24. Kaulen, A. D., and N. V. Postanogova. 1990. pH dependence of the dark equilibrium between 13-cis- and trans-bacteriorhodopsins of purple membranes. Biokhimiia. 55:516-519.
25. Kimura, Y., A. Ikegami, and W. Stoeckenius. 1984. Salt and pH-dependent changes of the purple membrane absorption spectrum. Photochem. Photobiol. 40:641-646.
26. Kouyama, T., R. A. Bogomolni, and W. Stoeckenius. 1985. Photoconversion from the light-adapted to the dark-adapted state of bacteriorhodopsin. Biophys. J. 48:201-208.
27. Lanyi, J. K. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta. 1183: 241-261.
28. Litvin, F. F., and S. P. Balashov. 1977. New intermediates in the photochemical conversions of bacteriorhodopsin. Biophysics. 22:1157-1160.
29. Liu, S. Y., M. Kono, and T. G. Ebrey. 1991. Effect of buffer molecules on the light-induced currents from oriented purple membrane. Biophys. J. 60:204-216.
30. Maeda, A., and T. Yoshizawa. 1980. Formation of 9-cis and 11-cis-retinal pigments from bacteriorhodopsin by irradiating purple membrane in acid. Biochemistry. 19:3825-3831.
31. Mathies, R. A., S. W. Lin, J. B. Ames, and W. T. Pollard. 1991. From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump. Annu. Rev. Biophys. Chem. 20:491-518.
32. 13C CP-MAS NMR investigation. FEBS Lett. 303:237-241.
33. 13C]Asp resonances. Biochemistry. 31:455-462.
34. Moore, T, A., M. E. Edgerton, G. Parr, C. Greenwood, and R. N. Perham. 1978. Studies of an acid-induced species of purple membrane from Halobacterium halobium. Biochem. J. 171:469-476.
35. Mowery, P. C., R. H. Lozier, Q. Chae, Y.-W. Tseng, M. Taylor, and W. Stoeckenius. 1979. Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry. 18:4100-4107.
36. Nasuda-Kouyama, A., K. Fukuda, T. Iio, and T. Kouyama. 1990. Effect of a light induced pH gradient on purple-to-blue and purple-to-red transitions of bacleriorhodopsin. Biochemistry. 29:6778-6788.
37. Oesterhelt, D., M. Meentzen, and L. Schuhmann. 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.
38. Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature. 233:149-152.
39. Ohno, H., Y. Takeuchi, and M. Yoshida. 1977. Effect of light-adaptation on the photoreaction of bacteriorhodopsin from Halobacterium halobium. Biochim. Biophys. Acta. 462:575-582.
40. Ohtani, H., T. Kobayashi, J.-I. Iwai, and A. Ikegami. 1986. Picosecond and nanosecond spectroscopies of the photochemical cycles of acidified bacteriorhodopsin. Biochemistry. 25:3356-3363.
41. Pande, C., R. H. Callender, C.-H. Chang, and T. G. Ebrey. 1985. Resonance Raman spectra of the "blue" and the regenerated "purple" membranes of Halobacterium halobium. Photochem. Photobiol. 42:549-552.
42. Rath, P., M. P. Krebs, Y. He, H. G. Khorana, and K. J. Rothschild. 1993. Fourier transform Raman spectroscopy of the bacteriorhodopsin mutant Tyr-185→ Phe: formation of a stable O-like species during lightadaptation and detection of its transient N-like photoproduct. Biochemistry. 32:2272-2281.
43. a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:4054-4062.
44. 548 and its primary photoproduct. J Biol. Chem. 263:5110-5117.
45. Rothschild, K. J. 1992. FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model. J Bioenerg. Biomembr. 24:147-167.
46. Scharnagl, C., J. Hettenkofer, and S. F. Fischer. 1994. Proton release pathway in bacteriorhodopsin: molecular dynamics and electrostatic calculations. Int. J. Quant. Chem. S21:33-56.
47. Scherrer, P., W. Stoeckenius, M. K. Mathew, and W. Sperling. 1987. Isomer ratio in dark-adapted bacteriorhodopsin. In Biophysical Studies of Retinal Proteins. T. G. Ebrey, H. Frauenfelder, B. Honig, and K. Nakanishi, editors. University of Illinois Press, Urbana-Champaign, IL. 206-211.
48. Schulte, A., L. Bradley II, and C. Williams. 1995. Equilibrium composition of retinal isomers in dark-adapted bacteriorhodopsin and effect of high pressure probed by near-infrared Raman spectroscopy. Appl. Spectrosc, 49:80-83.
49. Sharp, K. A., and B. Honig. 1990. Electrostatic interactions in macromolecules: theory and applications. Annu. Rev. Biophys. Chem. 19:301-332.
50. Smith, S. O, and R. A. Mathies. 1985. Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin. Biophys. J. 47: 251-254.
51. 570 and an O-like species. Biochemistry. 32:2263-2271.
52. Song, L., M. A. El-Sayed, and J. K. Lanyi. 1993. Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacterial photosynthesis. Science. 261:891-894.
53. Song, L., D. Yang, M. A. El-Sayed, and J. K. Lanyi. 1995. Retinal isomer composition in some bacteriorhodopsin mutants under light and dark adaptation conditions. J. Phys. Chem. 99:10052-10055.
54. Sperling, W., P. Carl, Ch. N. Rafferty, and N. A. Dencher. 1977. Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers. Biophys. Struct. Mech. 3:79-84.
55. Subramaniam, S., T. Marti, and H. G. Khorana. 1990. Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82-→Ala and Asp-85→Glu: the blue form is inactive in proton translocation. Proc. Natl. Acad. Sci. USA. 87:1013-1017.
56. Thompson, L. K., A. E. McDermott, J. Raap, C. M. van der Wielen, J. Lugtenburg, J. Herzfeld, and R. G. Griffin. 1992. Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage. Biochemistry. 31:7931-7938.
57. Tsuda, M., M. Glaccum, B. Nelson, and T. G. Ebrey. 1980. Light isomerizes the chromophore of bacteriorhodopsin. Nature. 287:351-353.
58. Turner, G. J., L. J. W. Miercke, T. E. Thorgeirsson, D. S. Kliger, M. C. Betlach, and R. M. Stroud. 1993. Bacteriorhodopsin D85N: three spectroscopic species in equilibrium. Biochemistry. 32:1332-1337.
59. Varo, G., and J. K. Lanyi. 1989. Photoreactions of bacteriorhodopsin at acid pH. Biophys. J. 56:1143-1151.
60. Warshel, A., and M. Ottolenghi. 1979. Kinetic and spectroscopic effects of protein-chromophore electrostatic interaction in bacteriorhodopsin. Photochem. Photobiol. 30:291-293.