Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR

Biophysical Journal

Volumn 76, Issue 3, 1999, Pages 1523-1531

  Tuzi, Satoru ^a   Yamaguchi, Satoru ^a   Tanio, Michikazu ^a   Konishi, Hidemasa ^a   Inoue, Sayuri ^a   Naito, Akira ^a   Needleman, Richard ^b   Lanyi, Janos K ^c   Saitô, Hazime ^a  

^a UNIVERSITY OF HYOGO   (Japan)

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

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; CALCIUM ION; CATION; MANGANESE; SODIUM ION;

ARTICLE; BINDING AFFINITY; BINDING SITE; CRYOELECTRON MICROSCOPY; PH; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; X RAY DIFFRACTION;

BACTERIA (MICROORGANISMS);

EID: 0033058935     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77311-X     Document Type: Article

References (54)

1. Ariki, M, and J. K. Lanyi. 1986. Characterization of metal ion-binding sites in bacteriorhodopsin. J. Biol. Chem. 261:8167-8174.
2. 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.
3. Chang, C. H., J. G. Chen, R. Govindjee, and T. Ebrey. 1985. Cation binding by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 82:396-400.
4. Chang, C. H., R. Jonas, S. Melchiore, R. Govindjee, and T. G. Ebrey. 1986. Mechanism and role of divalent cation binding of bacteriorhodopsin. Biophys. J. 49:731-739.
5. Corcoran, T. C., K. Z. Ismail, and M. A. El-Sayed. 1987. Evidence for the involvement of more than one metal cation in the Schiff base deprotonation process during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 84:4094-4098.
6. Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saitô, Y. Kimura, R. Needleman, and J. K. Lanyi. 1998. Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry. 37: 2496-2506.
7. Dunach, M., E. Padrós, A. Muga, and J. L. Arrondo. 1989. Fourier-transform infrared studies on cation binding to native and modified purple membranes. Biochemistry. 28:8940-8945.
8. Dunach, M., E. Padrós, M. Seigneuret, and J. L. Rigaud. 1988a. On the molecular mechanism of the blue to purple transition of bacteriorhodopsin. J. Biol. Chem. 263:7555-7559.
9. Dunach, M., M. Seigneuret, J. L. Rigaud, and E. Padrós. 1988b. Influence of cations on the blue to purple transition of bacteriorhodopsin. J. Biol. Chem. 263:17378-17384.
10. Dunach, M., M. Seigneuret, J. L. Rigaud, and E. Padrós. 1987. Characterization of the cation binding sites of the purple membrane. Electron spin resonance and flash photolysis studies. Biochemistry. 26:1179-1186.
11. Engelhard, M., B. Hess, M. Chance, and B. Chance. 1987. X-ray absorption studies on bacteriorhodopsin. FEBS Lett. 222:275-278.
12. Engelhard, M., B. Pevec, and B. Hess. 1989. Modification of two peptides of bacteriorhodopsin with a pentaamminecobalt(III) complex. Biochemistry. 28:5432-5438.
13. Fischer, U., and D. Oesterhelt. 1979. Chromophore equilibria in bacteriorhodopsin. Biophys. J. 28:211-230.
14. Fu, X., S. Bressler, M. Ottolenghi, T. Eliash, N. Friedman, and M. Sheves. 1997. Titration kinetics of Asp-85 in bacteriorhodopsin: exclusion of the retinal pocket as the color-controlling cation binding site. FEBS Lett. 416:167-170.
15. Griffiths, J. A., M. A. El-Sayed, and M. Capel. 1996a. Effect of binding of lanthanide ions on bacteriorhodopsin hexagonal structure: an x-ray study. J. Phys. Chem. 100:12002-12007.
16. 2 in bacteriorhodopsin. J. Phys. Chem. 100:6863-6866.
17. Grigorieff, N., T. A. Ceska, K. H. Downing, J. M. Baldwin, and R. Henderson. 1996. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259:393-421.
18. 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.
19. Kimura, Y., A. Ikegami, and W. Stoeckenius. 1984. Salt and pH-dependent changes of the purple membrane absorption spectrum. Photochem. Photobiol. 40:641-646.
20. Lanyi, J. K. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta. 1183: 241-261.
21. Lanyi, J. K. 1997. Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272: 31209-31212.
22. Luecke, H., H. T. Richter, and J. K. Lanyi. 1998. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science. 280: 1934-1937.
23. 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. Biophys. Chem. 20:491-518.
24. 85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. FEBS Lett. 303:237-241.
25. Mitra, A. K., and R. M. Stroud. 1990. High sensitivity electron diffraction analysis. A study of divalent cation binding to purple membrane. Biophys. J. 57:301-311.
26. 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.
27. Mowery, P. C., R. H. Lozier, Q. Chae, Y. Tseng, M. Taylor, and W. Stoeckenius. 1979. Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry. 18:4100-1407.
28. 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.
29. Onishi, H., M. E. McCance, and N. E. Gibbons. 1965. A synthetic medium for extremely halophilic bacteria. Can. J. Microbiol. 11:365-373.
30. Ovchinnikov, Y. A. 1982. Rhodopsin and bacteriorhodopsin: structure-function relationships. FEBS Lett. 148:179-191.
31. 3+ binding site in regenerated bacteriorhodopsin that is coordinated with the protein and phospholipid head groups. Proc. Natl. Acad. Sci. USA. 93:14333-14337.
32. 13C chemical shifts: a new means of conformational characterization as obtained by high-resolution solid-state NMR. Magn. Reson. Chem. 24:835-852.
33. Saitô, H., and I. Ando. 1989. High-resolution solid-state NMR studies of synthetic and biological macromolecules. Annu. Rep. NMR Spectrosc. 21:209-290.
34. Sepulcre, F., J. Cladera, J. Garcia, M. G. Proietti, J. Torres, and E. Padrós. 1996. An extended x-ray absorption fine structure study of the high-affinity cation-binding site in the purple membrane. Biophys. J. 70: 852-856.
35. Stoeckenius, W., and R. A. Bogomolni. 1982. Bacteriorhodopsin and related pigments of halobacteria. Annu. Rev. Biochem. 52:587-616.
36. 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.
37. 3+-regenerated bacteriorhodopsin. FEBS Lett. 282:436-440.
38. Szundi, I., and W. Stoeckenius. 1987. Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 84:3681-3684.
39. Szundi, I., and W. Stoeckenius. 1989. Surface pH controls purple-to-blue transition of bacteriorhodopsin. Biophys. J. 56:369-383.
40. 13C NMR. Biochim. Biophys. Acta. 1375:84-92.
41. 13C magnetic resonance. Biopolymers. 13:97-114.
42. 13C]Leu and Val-labelled bacteriorhodopsin. Eur. J. Biochem. 218:837-844.
43. 13C] Ala-labeled bacteriorhodopsin. Biochemistry. 33:15046-15052.
44. 13C NMR. Eur. J. Biochem. 239:294-301.
45. 13C nuclear magnetic resonance. Biochemistry. 35:7520-7527.
46. 2+, in regenerated bacteriorhodopsin. J. Phys. Chem. 98:7246-7251.
47. Wu, S., and M. A. El-Sayed. 1994b. Binding of, and energy-transfer studies from retinal to, organic cations in regenerated reduced bacteriorhodopsin. J. Phys. Chem. 98:9339-9344.
48. 13C NMR. J. Biochem. (Tokyo). 123: 78-86.
49. 2+ binding to deionized monomerized and to retinal removed bacteriorhodopsin. Biophys. J. 69:2056-2059.
50. 2+ to the two high-affinity sites of bacteriorhodopsin. J. Phys. Chem. 99:11600-11604.
51. - ions. Biophys. J. 73:2097-2105.
52. 2+ low-affinity binding sites in bacteriorhodopsin. Biochemistry. 32: 14173-14175.
53. 2+ binding to deionized bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 90:1445-1449.
54. 2+-regenerated bacteriorhodopsin. Biophys. J. 61:1201-1206.