Dissection of environmental changes at the cytoplasmic surface of light-activated bacteriorhodopsin and visual rhodopsin: Sequence of spectrally silent steps

Photochemistry and Photobiology

Volumn 85, Issue 2, 2009, Pages 570-577

  Kim, Tai Yang ^a   Moeller, Martina ^a   Winkler, Kathrin ^a   Kirchberg, Kristina ^a   Alexiev, Ulrike ^a  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; RHODOPSIN;

CHEMISTRY; CONFERENCE PAPER; CYTOPLASM; HALOBACTERIUM SALINARUM; KINETICS; LIGHT; RADIATION EXPOSURE; SPECTROPHOTOMETRY; TIME;

BACTERIORHODOPSINS; CYTOPLASM; HALOBACTERIUM SALINARUM; KINETICS; LIGHT; RHODOPSIN; SPECTROPHOTOMETRY; TIME FACTORS;

EID: 60849087699     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2008.00525.x     Document Type: Conference Paper

References (34)

1. Radzwill, N., K. Gerwert H. J. Steinhoff (2001) Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin. Biophys. J. 80, 2856 2866.
2. Pieper, J., A. Buchsteiner, N. A. Dencher, R. E. Lechner T. Hauss (2008) Transient protein softening during the working cycle of a molecular machine. Phys. Rev. Lett. 100, 228103.
3. Mielke, T., U. Alexiev, M. Gläsel, H. Otto M. P. Heyn (2002) Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII-state. Biochemistry 41, 7875 7884.
4. Alexiev, U., I. Rimke T. Pöhlmann (2003) Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study. J. Mol. Biol. 328, 705 719.
5. Kim, T.-Y., K. Winkler U. Alexiev (2007) Picosecond multidimensional fluorescence spectroscopy: A tool to measure real-time protein dynamics during function. Photochem. Photobiol. 83, 378 384.
6. Dunham, T. D. D. L. Farrens (1999) Conformational changes in rhodopsin. Movement of helix F detected by site-specific chemical labeling and fluorescence spectroscopy. J. Biol. Chem. 274, 1683 1690.
7. Imamoto, Y., M. Kataoka, F. Tokunaga K. Palczewski (2000) Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface. Biochemistry 39, 15225 15233.
8. Lehmann, N., U. Alexiev K. Fahmy (2007) Linkage between the intramembrane H-bond network around aspartic acid 83 and the cytosolic environment of helix 8 in photoactivated rhodopsin. J. Mol. Biol. 366, 1129 1141.
9. Moltke, S., U. Alexiev M. P. Heyn (1995) Kinetics of light induced intramolecular charge transfer and proton release in bacteriorhodopsin. Isr. J. Chem. 35, 401 414.
10. Subramaniam, S. R. Henderson (2000) Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406, 653 657.
11. Alexiev, U., R. Mollaaghababa, P. Scherrer, H. G. Khorana 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.
12. Otto, H., T. Marti, M. Holz, T. Mogi, M. Lindau, H. G. Khorana M. P. 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.
13. Bennett, N. (1980) Optical study of the light-induced protonation changes associated with the metarhodopsin II intermediate in rod-outer-segment membranes. Eur. J. Biochem. 111, 99 103.
14. Arnis, S. K. P. Hofmann (1993) Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl Acad. Sci. USA 90, 7849 7853.
15. Sass, H. J., G. Bueldt, R. Gessenich, D. Hehn, D. Neff, R. Schlesinger, J. Berendzen P. Ormos (2000) Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature 406, 649 653.
16. Knierim, B., K. P. Hofmann, O. P. Ernst W. L. Hubbell (2007) Sequence of late molecular events in the activation of rhodopsin. Proc. Natl Acad. Sci. USA 104, 20290 20295.
17. Park, J. H., P. Scheerer, K. P. Hofmann, H. W. Choe O. P. Ernst (2008) Crystal structure of the ligand free G-protein coupled receptor opsin. Nature 454, 183 187.
18. Krebs, M. P., R. Mollaaghababa H. G. Khorana (1993) Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants. Proc. Natl Acad. Sci. USA 90, 1987 1991.
19. Mcdowell, J. H. H. Kuhn (1977) Light-induced phosphorylation of rhodopsin in cattle photoreceptor membranes: substrate activation and inactivation. Biochemistry 16, 4054 4060.
20. Fung, B. K. W. L. Hubbell (1978) Organization of rhodopsin in photoreceptor membranes. 1. Proteolysis of bovine rhodopsin in native membranes and the distribution of sulfhydryl groups in the fragments. Biochemistry 17, 4396 4402.
21. Blazynski, C. S. E. Ostroy (1981) Dual pathways in the photolysis of rhodopsin: Studies using a direct chemical method. Vision Res. 21, 833 841.
22. Sakmar, T. P., R. R. Franke H. G. Khorana (1989) Glutamic acid-113 serves as the retinylidene Schiff base counter ion in bovine rhodopsin. Proc. Natl Acad. Sci. USA 86, 8309 8313.
23. Farrens, D. L. H. G. Khorana (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5070 5076.
24. Schröder, G., U. Alexiev H. Grubmüller (2005) Simulation of fluorescence anisotropy experiments: Probing protein dynamics. Biophys. J. 89, 3757 3770.
25. Kuwata, O., C. Yuan, S. Misra, R. Govindjee T. G. Ebrey (2001) Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: Possible coupling to proton uptake and formation of the active form of Meta II. Biochemistry (Mosc.) 66, 1283 1299.
26. Alexiev, U., P. Scherrer, T. Marti, H. G. Khorana M. P. Heyn (1995) Time-resolved surface charge change at the cytoplasmic side of bacteriorhodopsin. FEBS Lett. 373, 81 84.
27. Mollaaghababa, R., H. J. Steinhoff, W. L. Hubbell H. G. Khorana (2000) Time-resolved site-directed spin-labeling studies of bacteriorhodopsin: Loop-specific conformational changes in M. Biochemistry 39, 1120 1127.
28. Altenbach, C., A. K. Kusnetzow, O. P. Ernst, K. P. Hofmann W. L. Hubbell (2008) High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl Acad. Sci. USA 105, 7439 7444.
29. Lanyi, J. B. Schobert (2006) Propagating structural perturbation inside bacteriorhodopsin: Crystal structures of the M state and the D96A and T46V mutants. Biochemistry 45, 12003 12010.
30. Garczarek, F. L. Brown., J. K. Lanyi K. Gerwert (2005) Proton binding within a membrane protein by a protonated water cluster. Proc. Natl Acad. Sci. USA 102, 3633 3638.
31. Rink, T., M. Pfeiffer, D. Oesterhelt, K. Gerwert H.-J. Steinhoff (2000) Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy. Biophys. J. 78, 1519 1530.
32. Subramaniam, S., M. Lindahl, P. Bullough, A. R. Faruqi, J. Tittor, D. Oesterhelt, L. Brown, J. Lanyi R. Henderson (1999) Protein conformational changes in the bacteriorhodopsin photocycle. J. Mol. Biol. 287, 145 161.
33. Oka T., N. Yagi., F. Tokunaga M. Kataoka (2002) Time-resolved X-ray diffraction reveals movement of F helix of D96N bacteriorhodopsin during M-MN transition at neutral pH. Biophys. J. 82, 2610 2616.
34. Luecke, H., B. Schobert, H.-T. Richter, J.-P. Cartailler J. K. Lanyi (1999) Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 286, 255 260.