Evidence for a controlling role of water in producing the native bacteriorhodopsin structure

Biophysical Journal

Volumn 73, Issue 4, 1997, Pages 2081-2089

  Rousso, I ^a   Friedman, N ^a   Lewis, A ^b   Sheves, M ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; WATER;

ABSORPTION SPECTROSCOPY; ARTICLE; HALOBACTERIUM; INFRARED SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PURPLE MEMBRANE;

HALOBACTERIUM;

EID: 0030823235     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78238-9     Document Type: Article

References (42)

1. 13C NMR studies of model compounds for bacteriorhodopsin: factors affecting the retinal chromophore chemical shifts and absorption maximum. J. Am. Chem. Soc. 114:2400-2411.
2. Baasov, T., and M. Sheves. 1985. Model compounds for the study of spectroscopic properties of visual pigments and bacteriorhodopsin. J. Am. Chem. Soc. 107:7524-7533.
3. Balashov, S., R. Govindjee, M. Kono, E. Imasheva, E. Lukashev, T. Ebrey, R. Crouch, D. Menick, and Y. Feng. 1993. Effect of the arginine 82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release and photochemical cycle. Biochemistry. 32:10331-10343.
4. Brown, L., J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J. Lanyi. 1995. Glutamic acid 204 is the thermal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270: 27122-27126.
5. Butt, H., K. Fendler, A. Der, and E. Bamberg. 1984. Temperature jump study of charge translocation during the bacteriorhodopsin photocycle. Biophys. J. 56:851-859.
6. Cao, Y., G. Varo, M. Chang, B. Ni, R. Needleman, and J. Lanyi. 1991. Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base. Biochemistry. 30:10972-10979.
7. 15N shift anisotropy. Biochemistry. 28:3346-3353.
8. Dupuis, P., I. Harosi, C. Sandorfy, J. Leclerq, and D. Vocelles. 1980. First step in vision: proton transfer or isomerization. Rev. Can. Biol. 39: 247-258.
9. a of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem. Soc. 115:3772-3773.
10. Gerwert, K., B. Hess, and M. Engelhard. 1990. Porline residues undergo structural changes during proton pumping in bacteriorhodopsin. FEBS Lett. 261:449-454.
11. Gerwert, K., B. Hess, J. Sopa, and D. Oesterhelt. 1989. Role of aspartate-96 in proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 86:4943-4947.
12. Grigorieff, N., T. Ceska, K. Downing, J. Baldwin, and R. Henderson. 1996. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259:393-421.
13. Harbison, G., J. Herzfeld, and R. Griffin. 1983. Solid state nitrogen-15 nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin. Biochemistry. 22:1-5.
14. 13C NMR detection of a perturbed 6-s-trans chromopore in bacteriorhodopsin. Biochemistry. 24: 6955-6962.
15. Hildebrand, P., and M. Stockburger. 1984. Role of water in bacteriorhodopsin's chromophore: resonance Raman study. Biochemistry. 23: 5539-5548.
16. Holz, M., L. Drachev, T. Mogi, H. Otto, A. Kaulen, M. Heyn, V. Skulachev, and H. Khorana. 1989. Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement. Proc. Natl. Acad. Sci. USA. 86: 2167-2171.
17. Honig, B., M. Ottolenghi, and M. Sheves. 1995. Acid-base equilibria and the proton pump in bacteriorhodopsin. Isr. J. Chem. 35:429-446.
18. Hu, J., G. Griffin, and J. Herzfeld. 1994. Synergy in the spectral tuning of retinal pigments: complete accounting of the opsin shift in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 91:8880-8884.
19. Humphrey, W., I. Logunov, K. Schulten, and M. Sheves. 1994. Molecular dynamics study of bacteriorhodopsin and artificial pigments. Biochemistry. 33:3668-3678.
20. Korenstein, R., and B. Hess 1977. Hydration effect on the photocycle of bacteriorhodopsin in thin layers of purple membrane. Nature. 270: 184-186.
21. Lanyi, J., and G. Varo 1995. The photocycle of bacteriorhodopsin. Isr. J. Chem. 35:365-386.
22. Maeda, A., J. Sasaki, Y. Yamazaki, R. Needleman, and J. Lanyi. 1994. Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study. Biochemistry. 33:1713-1717.
23. Oesterhelt, D., and W. Stoeckenius 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233: 149-152.
24. Oesterhelt, D., and W. Stoeckenius 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678.
25. Otto, H., T. Marti, M. Holz, T. Mogi, M. Lindau, H. Khorana, and M. Heyn. 1989. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 86:9228-9232.
26. Papadopoulos, G., N. Dencher, G. Zaccai, and G. Buldt. 1990. Water molecules and exchangeable hydrogen ions at the active center of bacteriorhodopsin localized by neutron diffraction. J. Mol. Biol. 214: 15-19.
27. Rousso, I., I. Brodsky, A. Lewis, and M. Sheves. 1995a. The role of water in retinal complexation to bacterioopsin. J. Biol. Chem. 270: 13860-13868.
28. a of the protonated Schiff base and Asp 85 in the bacteriorhodopsin binding site is controlled by a specific geometry between the two residues. Biochemistry. 34:10259-10265.
29. Rousso, I., M. Sheves, and A. Lewis. 1996. Protein structure alteration induced by light-activated water absorption. A study with bacteriorhodopsin. J. Am. Chem. Soc. 118:11299-11300.
30. Rüdiger, M., J. Tittor, K. Gerwert, and D. Oesterhelt. 1997. Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectroscopy. Biochemistry. 36:4867-4874.
31. Sampogna, R., and B. Honig. 1994. Environmental effects on the protonation states of active site residues in bacteriorhodopsin. Biophys. J. 66:1341-1352.
32. Schreckenbach, T., B. Walckhoff, and D. Oesterhelt. 1977. Studies on the retinal-protein interaction in bacteriorhodopsin. J. Biochem. (Tokyo). 76:499-511.
33. Schreckenbach, T., B. Walckhoff, and D. Oesterhelt. 1978. Specificity of the retinal binding site of bacteriorhodopsin: chemical and stereochemical requirements for the binding of retinol and retinal. Biochemistry. 17:5353-5359.
34. Schweiger, V., J. Tittor, and D. Oesterhelt. 1994. Bacteriorhodopsin can function without a covalent linkage between retinal and protein. Biochemistry. 33:535-541.
35. a of the bacteriorhodopsin Schiff base by use of artificial retinal analogues. Proc. Natl. Acad. Sci. U.S.A. 83:3262-3266.
36. Sheves, M., N. Friedman, A. Albeck, and M. Ottolenghi. 1985. Primary photochemical event in bacteriorhodopsin: study with artificial pigments. Biochemistry. 24:1260-1265.
37. Spudich, T., D. McCain, K. Nakanishi, M. Okabe, N. Shimizer, H. Rodman, B. Honig, and R. Bogomolni. 1986. Chromophore-protein interaction in bacterial sensory rhodopsin and bacteriorhodopsin. Biophys. J. 49:479-483.
38. Stern, L., P. Ahl, T. Marti, T. Mogi, M. Dunach, S. Berkowitz, K. Rothschild, and H. Khorana. 1989. Structure-function studies on bacteriorhodopsin. Substitution of membrane-embedded aspartic acids in bacteriorhodopsin causes specific changes in different steps of the photochemical cycle. Biochemistry. 28:10035-10042.
39. Takei, H., Y. Gat, Z. Rothman, A. Lewis, and M. Sheves. 1994. Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle. J. Biol. Chem. 269:7387-7389.
40. Tittor, J., C. Snell, D. Oesterhelt, H. Butt, and E. Bamberg. 1989. A defective proton pump, point-mutated bacteriorhodopsin Asp 96-Asn is fully reactivated by azide. EMBO J. 8:3477-3482.
41. Varo, G., and L. Keszthelyi. 1983. Photoelectric signals from dried oriented purple membranes of Halobacterium halobium. Biophys. J. 43: 47-51.
42. Xu, D., M. Sheves, and K. Schulten. 1995. Molecular dynamics study of the M intermediate of bacteriorhodopsin. Biophys. J. 69:2745-2760.