The effect of chemical additives on the bacteriorhodopsin photocycle

Journal of Photochemistry and Photobiology B: Biology

Volumn 49, Issue 2-3, 1999, Pages 192-197

  Batori Tartsi, Zita ^a   Ludmann, Krisztina ^b   Váró, György ^b  

^a UZHGOROD NATIONAL UNIVERSITY   (Ukraine)

^b INSTITUTE OF BIOCHEMISTRY   (Hungary)

Author keywords

Absorption kinetics; Gelatin; Humidity; Model fitting; Mutants; Triethanolamine

Indexed keywords

BACTERIORHODOPSIN; GELATIN; TRIETHANOLAMINE;

ABSORPTION SPECTROSCOPY; ARTICLE; BACTERIUM MUTANT; CONTROLLED STUDY; HUMIDITY; NONHUMAN; PHOTOCHEMISTRY; PRIORITY JOURNAL; PURPLE MEMBRANE; WATER CONTENT;

EID: 0033120305     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(99)00058-5     Document Type: Article

References (49)

1. R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, K.H. Downing, Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy, J. Mol. Biol. 213 (1990) 899-929.
2. H. Luecke, H.T. Richter, J.K. Lanyi, Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution, Science 280 (1998) 1934-1937.
3. G. Váró, J.K. Lanyi, Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle, Biochemistry 34 (1995) 12161-12169.
4. G.S. Harbison, S.O. Smith, J.A. Pardoen, C. Winkel, J. Lugtenburg, J. Herzfeld, R.A. Mathies, R.G. Griffin, Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases, Proc. Natl. Acad. Sci. USA 81 (1984) 1706-1709.
5. T.G. Ebrey, Light energy transduction in bacteriorhodopsin, in: M. Jackson (Ed.), Thermodynamics of Membranes, Receptors and Channels, CRC Press, New York, 1993, pp. 353-387.
6. M.P. Krebs, H. Gobind Khorana, Mechanism of light-dependent proton translocation by bacteriorhodopsin, J. Bacteriol. 175 (1993) 1555-1560.
7. U. Haupts, J. Tittor, E. Bamberg, D. Oesterhelt, General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model, Biochemistry 36 (1997) 2-7.
8. C. Gergely, L. Zimányi, G. Váró, Bacteriorhodopsin intermediate spectra determined over a wide pH range, J. Phys. Chem. B 101 (1997) 9390-9395.
9. A. Lewis, J.P. Spoonhower, R.A. Bogomolni, R.H. Lozier, W. Stoeckenius, Tunable laser resonance Raman spectroscopy of bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 71 (1974) 4462-4466.
10. M.A. Marcus, A. Lewis, Kinetic resonance Raman spectroscopy: Dynamics of deprotonation of the Schiff base of bacteriorhodopsin, Science 195 (1977) 1328-1330.
11. T. Mogi, L.J. Stern, N.R. Hackett, H.G. Khorana, Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation, Proc. Natl. Acad. Sci. USA 84 (1987) 5595-5599.
12. T Mogi, L.J. Stern, T. Marti, B.H. Chao, H.G. Khorana, Aspartic acid substitutions affect proton translocation by bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 85 (1988) 4148-4152.
13. B. Ni, M. Chang, A. Duschl, J.K. Lanyi, R. Needleman, An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium, Gene 90 (1990) 169-172.
14. T.E. Thorgeirsson, S.J. Milder, L.J.W. Miercke, M.C. Betlach, R.F. Shand, R.M. Stroud, D.S. Kliger, Effects of Asp-96 → Asn, Asp-85 → Asn, and Arg-82 → Gln single-site substitutions on the photocycle of bacteriorhodopsin, Biochemistry 30 (1991) 9133-9142.
15. L.S. Brown, J. Sasaki, H. Kandori, A. Maeda, R. Needleman, J.K. Lanyi, Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin, J. Biol. Chem. 270 (1995) 27122-27126.
16. A.K. Dioumaev, H.T. Richter, L.S. Brown, M. Tanio, S. Tuzi, H. Saito, Y. Kimura, R. Needleman, J.K. Lanyi, Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface, Biochemistry 37 (1998) 2496-2506.
17. M. Holz, L.A. Drachev, T. Mogi, H. Otto, A.D. Kaulen, M.P. Heyn, V.P. Skulachev, H.G. Khorana, 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 (1989) 2167-2171.
18. Y. Cao, G. Váró, M. Chang, B. Ni, R. Needleman, J.K. Lanyi, Water is required for proton transfer from aspartate 96 to the bacteriorhodopsin Schiff base, Biochemistry 30 (1991) 10972-10979.
19. Z. Dancsházy, R. Govindjee, T.G. Ebrey, Independent photocycles of the spectrally distinct forms of bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 85 (1988) 6358-6361.
20. W. Eisfeld, C. Pusch, R. Diller, R. Lohrmann, M. Stockburger, Resonance Raman and optical transient studies on the light-induced proton pump of bacteriorhodopsin reveal parallel photocycles, Biochemistry 32 (1993) 7196-7215.
21. L. Song, S.L. Logunov, D. Yang, M.A. El-Sayed, The pH dependence of the subpicosecond retinal photoisomerization process in bacteriorhodopsin: Evidence for parallel photocycles, Biophys. J. 67 (1994) 2008-2012.
22. J.B. Ames, R.A. Mathies, The role of back-reactions and proton uptake during the N → O transition in bacteriorhodopsin's photocycle: A kinetic resonance Raman study, Biochemistry 29 (1990) 7181-7190.
23. G. Váró, J.K. Lanyi, Pathways of the rise and decay of the M photointermediate of bacteriorhodopsin, Biochemistry 29 (1990) 2241-2250.
24. B. Hessling, G. Souvignier, K. Gerwert, A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates, Biophys. J. 65 (1993) 1929-1941.
25. I.V. Chizhov, D.S. Chernavskii, M. Engelhard, K.H. Mueller, B.V. Zubov, B. Hess, Spectrally silent transitions in the bacteriorhodopsin photocycle, Biophys. J. 71 (1996) 2329-2345.
26. S. Subramaniam, M. Gerstein, D. Oesterhelt, R. Henderson, Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin, EMBO J. 12 (1993) 1-8.
27. N. Friedman, Y. Gat, M. Sheves, M. Ottolenghi, On the heterogeneity of the M population in the photocycle of bacteriorhodopsin, Biochemistry 33 (1994) 14758-14767.
28. B.-G. Han, J. Vonck, R.M. Glaeser, The bacteriorhodopsin photocycle: Direct structural study of two substates of the M-intermediate, Biophys. J. 67 (1994) 1179-1186.
29. G. Váró, L. Eisenstein, Infrared studies of water induced conformational changes in bacteriorhodopsin, Eur. J. Biochem. 14 (1987) 163-168.
30. G. Papadopoulos, N.A. Dencher, G. Zaccai, G. Büldt, Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway, J. Mol. Biol. 214 (1990) 15-19.
31. H. Deng, L. Huang, R. Callender, T.G. Ebrey, Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: A resonance Raman study of the Schiff base hydrogen/deuterium exchange, Biophys. J. 66 (1994) 1129-1136.
32. Y. Yamazaki, M. Hatanaka, H. Kandori, J. Sasaki, W.F.J. Karstens, J. Raap, J. Lugtenburg, M. Bizounok, J. Herzfeld, R. Needleman, J.K. Lanyi, A. Maeda. Water structural changes at the proton uptake site (the Thr46-Asp96 domain) in the L intermediate of bacteriorhodopsin, Biochemistry 34 (1995) 7088-7093.
33. J. Fitter, R.E. Lechner, G. Büldt, N.A. Dencher, Internal molecular motions of bacteriorhodopsin: Hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes, Proc. Natl. Acad. Sci. USA 93 (1996) 7600-7605.
34. R. Korenstein, B. Hess, Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane, Nature 270 (1977) 184-186.
35. G. Váró, L. Keszthelyi, Photoelectric signals from dried oriented purple membranes of Halobacterium halobium, Biophys. J. 43 (1983) 47-51.
36. G. Váró, J.K. Lanyi, Distortions in the photocycle of bacteriorhodopsin at moderate dehydration, Biophys. J. 59 (1991) 313-322.
37. C. Ganea, C. Gergely, K. Ludmann, G. Váró, The role of water in the extracellular half channel of bacteriorhodopsin, Biophys. J. 73 (1997) 2718-2725.
38. P. Hildebrandt, M. Stockburger, Role of water in bacteriorhodopsin's chromophore: Resonance Raman study, Biochemistry 23 (1984) 5539-5548.
39. J.S. Jaffe, R.M. Glaeser, Difference Fourier analysis of 'surface features' of bacteriorhodopsin using glucose-embedded and frozen-hydrated purple membrane, Ultramicroscopy 23 (1987) 17-28.
40. G. Zaccai, Structure and hydration of purple membranes in different conditions, J. Mol. Biol. 194 (1987) 569-572.
41. C. Scharnagl, J. Hettenkofer, S.F. Fischer, Electrostatic and conformational effects on the proton translocation steps in bacteriorhodopsin: Analysis of multiple M structures, J. Phys. Chem. 99 (1995) 7787-7800.
42. 548) of bacteriorhodopsin and its photocycle, Biophys. J. 68 (1995) 1270-1282.
43. M. Yoshida, K. Ohno, Y. Takeuchi, Y. Kagawa, Prolonged lifetime of the 410-nm intermediate of bacteriorhodopsin in the presence of guanidine hydrochloride, Biochem. Biophys. Res. Commun. 75 (1977) 1111-1116.
44. I.K. Bandrovskaya, Y.D. Shershun, Z.I. Batori-Tartsi, N.P. Frolova, O.I. Korposh, J.P. Sharkany, Special photochrome material on the base of bacteriorhodopsin, SPIE Proc. 3055 (1997) 91-94.
45. D. Oesterhelt, W. Stoeckenius, Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane, Methods Enzymol. 31 (1974) 667-678.
46. R. Pethig, Water in biological systems, in: Dielectric and Electric Properties of Biological Materials, Wiley, New York, 1979.
47. L. Zimányi, J.K. Lanyi, Deriving the intermediate spectra and photocycle kinetics from time-resolved difference spectra of bacteriorhodopsin. The simpler case of the recombinant D96N protein, Biophys. J. 64 (1993) 240-251.
48. C. Gergely, C. Ganea, G.I. Groma, G. Váró, Study of the photocycle and charge motions of the bacteriorhodopsin mutant D96N, Biophys. J. 65 (1993) 2478-2483.
49. G. Váró, L. Keszthelyi, Arrhenius parameters of the bacteriorhodopsin photocycle in dried oriented samples, Biophys. J. 47 (1985) 243-246.