Perturbed interaction between residues 85 and 204 in Tyr-185→Phe and Asp-85→Glu bacteriorhodopsins

Biophysical Journal

Volumn 71, Issue 6, 1996, Pages 3392-3398

  Richter, Hans Thomas ^a   Needleman, Richard ^b   Lanyi, Janos K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; GLUTAMINE; PHENYLALANINE; PROTEIN; TYROSINE;

ARTICLE; HALOBACTERIUM; LIGHT ADAPTATION; MUTATION; NONHUMAN; PH; PROTON TRANSPORT; SPECTROSCOPY; TITRIMETRY;

HALOBACTERIUM;

EID: 0029731742     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79532-2     Document Type: Article

References (35)

1. Balashov, S. P., R. Govindjee and T. G. Ebrey. 1991. Red shift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH. Biophys. J. 60:465-490.
2. 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.
3. a of Asp85 is higher in all-trans than in 13-cis bacteriorhodopsin. Biophys. J 68:A334.
4. 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.
5. 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.
6. Braiman, M. S., T. Mogi, T. Marti, L. J. Stem, H. G. Khorana, and K. J. Rothschild. 1988. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartate residues 85, 96, and 212. Biochemistry. 27:8516-8520.
7. Brown, L. S., L. Bonet, R. Needleman, and J. K. Lanyi. 1993. Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle. Biophys. J. 65:124-130.
8. 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.
9. Druckmann, S., M. Ottolenghi, A. Pande, J. Pande, and R. H. Callender. 1982. Acid-base equilibrium of the Schiff base in bacteriorhodopsin. Biochemistry. 21:4953-4959.
10. Duñach, M., S. Berkowitz, T. Marti, Y-W. He, S. Subramaniam, H. G. Khorana, and K. Rothschild. 1990. Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. J. Biol. Chem. 265:16978-16984.
11. Fischer, U., and D. Oesterhelt. 1979. Chromophore equilibria in bacteriorhodopsin. Biophys. J. 28:211-230.
12. Greenhalgh, D. A., S. Subramaniam, U. Alexiev, H. Otto, M. P. Heyn, and H. G. Khorana. 1992. Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin. J. Biol. Chem. 267:25734-25738.
13. 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.
14. Jonas, R., and T. G. Ebrey. 1991. Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 88:149-153.
15. 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: the reprotonation switch of bacteriorhodopsin. J. Mol. Biol. 243:621-638.
16. Lanyi, J. K., J. Tittor, G. Váró, G. Krippahl, and D. Oesterhelt. 1992. Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore. Biochim. Biophys. Acta. 1099:102-110.
17. Marti, T., S. J. Rösselet, H. Otto, M. P. Heyn, and H. G. Khorana. 1991. The retinylidene Schiff base counterion in bacteriorhodopsin. J. Biol. Chem. 266:18674-18683.
18. 13C CP-MAS NMR investigation. FEBS Lett. 303:237-241.
19. Miercke, L. J. W., M. C. Betlach, A. K. Mitra, R. F. Shand, S. K. Fong, and R. M. Stroud. 1991. Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: purification to homogeneity, pH dependence of pumping, and electron diffraction. Biochemistry. 30:3088-3098.
20. 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.
21. Needleman, R., M. Chang, B. Ni, G. Váró, J. Fornes, S. H. White, and J. K. Lanyi. 1991. Properties of asp212-asn bacteriorhodopsin suggest that asp212 and asp85 both participate in a counterion and proton acceptor complex near the Schiff base. J. Biol. Chem. 266:11478-11484.
22. Otto, H., T. Marti, M. Holz, T. Mogi, L. J. Stern, F. Engel, H. G. Khorana, and M. P. Heyn. 1990. Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base. Proc. Natl. Acad. Sci. USA. 87:1018-1022.
23. 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 light adaptation and detection of its transient N-like photoproduct. Biochemistry. 32:2272-2281.
24. a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:4054-4062.
25. Richter, H. T., R. Needleman H. Kandori, A. Maeda, and J. K. Lanyi. 1996b. Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle. Biochemistry. In press.
26. Scharnagl, C., J. Hettenkofer, and S. F. Fischer. 1995. Electrostatic and conformational effects on the proton translocation steps in bacteriorhodopsin: analysis of multiple M structures. J. Phys. Chem. 99:7787-7800.
27. Smith, S. O., and R. A. Mathies. 1985. Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin. Biophys. J. 47: 251-254.
28. Smith, S. O., A. B. Myers, J. A. Pardoen, C. Winkel, P. P. J. Mulder, J. Lugtenburg, and R. A. Mathies. 1984. Determination of retinal Schiff base configuration in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 81:2055-2059.
29. 570 and an O-like species. Biochemistry. 32:2263-2271.
30. Stern, L. J., and H. G. Khorana. 1989. Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation. J. Biol. Chem. 264:14202-14208.
31. Subramaniam, S., D. A. Greenhalgh, and H. G. Khorana. 1992. Aspartic acid 85 in bacteriorhodopsin functions both as proton acceptor and negative counterion to the Schiff base. J. Biol. Chem. 267:25730-25733.
32. 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.
33. Tittor, J., U. Schweiger, D. Oesterhelt, and E. Bamberg. 1994. Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,D96N. Biophys. J. 67:1682-1690.
34. Váró, G., and J. K. Lanyi. 1989. Photoreactions of bacteriorhodopsin at acid pH. Biophys. J. 56:1143-1151.
35. Váró, G., R. Needleman, and J. K. Lanyi. 1996. Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacterio-rhodopsin photocycle. Biophys. J. 70:461-467.