Studies of cation binding in ZnCl2-regenerated bacteriorhodopsin by x- ray absorption fine structures: Effects of removing water molecules and adding Cl- ions

Biophysical Journal

Volumn 73, Issue 4, 1997, Pages 2097-2105

  Zhang, Ke ^a   Song, Li ^b   Dong, Jun ^a   El Sayed, M A ^b  

^a Biostructures Institute   (United States)

^b GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; CATION; CHLORIDE ION; WATER; ZINC; ZINC CHLORIDE;

ARTICLE; HALOBACTERIUM; LIGAND BINDING; NONHUMAN; PHOTOSYNTHESIS; PROTEIN BINDING; PURPLE MEMBRANE; ROENTGEN SPECTROSCOPY;

HALOBACTERIUM;

EID: 0030848662     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78240-7     Document Type: Article

References (51)

1. Ariki, M., and J. K. Lanyi. 1986. Characterization of metal ion-binding sites in bacteriorhodopsin. J. Biol. Chem. 261:8167-8174.
2. Becher, B. M., and J. Y. Cassim. 1975. Improved isolation procedures for the purple membrane of Halobacterium halobium. Prep. Biochem. 5:161-178.
3. Braiman, M. S., T. Mogi, T. Marti, L. J. Stern, H. G. Khorana, and K. J. Rothschild. 1988. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry. 27:8516-8520.
4. Butt, H. J., K. Fendler, E. Bamberg, J. Tittor, and D. Oesterhelt. 1989. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J. 8:1657-1663.
5. Chang, C. H., J. G. Chen, R. Govindjee, and T. Ebrey. 1985. Cation binding by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 82:396-400.
6. 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.
7. Chronister, E. L., T. C. Corcoran, L. Song, and M. A. El-Sayed. 1986. On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. USA. 83: 8580-8584.
8. 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.
9. Crozier, E. D., J. J. Rehr, and R. R. Ingalls. 1988. Amorphous and liquid systems. In X-Ray Absorption: Principle, Application, Techniques of EXAFS, SEXAFS, and XANES. John Wiley and Sons, New York. 373.
10. Dencher, N. A., J. Heberle, C. Bark, M. H. J. Koch, G. Rapp, D. Oesterhelt, K. Bartels, and G. Bueldt. 1991. Proton translocation and conformational changes during the bacteriorhodopsin photocycle: time-resolved studies with membrane-bound optical probes and x-ray diffraction. Photochem. Photobiol. 54:881-887.
11. 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.
12. Dunach, M., E. Padros, M. Seigneuret, and J. L. Rigaud. 1988a. On the molecular mechanism of the blue to purple transition of bacteriorhodopsin. UV-difference spectroscopy and electron spin resonance studies. J. Biol. Chem. 263:7555-7559.
13. Dunach, M., M. Seigneuret, J. L. Rigaud, and E. Padros. 1987. Characterization of the cation binding sites of the purple membrane. Electron spin resonance and flash photolysis studies. Biochemistry. 26:1179-1186.
14. Dunach, M., M. Seigneuret, J. L. Rigaud, and E. Padros. 1988b. Influence of cations on the blue to purple transition of bacteriorhodopsin. Comparison of calcium and mercury(2+) binding and their effect on the surface potential. J. Biol. Chem. 263:17378-17384.
15. Englehard, M., B. Hess, M. Chance, and B. Chance. 1987. X-ray absorption studies on bacteriorhodopsin. FEBS Lett. 222:275-278.
16. Griffiths, J. A., J. King, R. Browner, and M. A. El-Sayed. 1996a. Calcium and magnesium binding in native and structurally perturbed purple membrane. J. Phys. Chem. 100:929-933.
17. - in bacteriorhodopsin. J. Phys. Chem. 100:6863-6866.
18. Heberle, J., and N. A. Dencher. 1992. Surface-bound optical probes monitor proton translocation and surface potential changes during the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. USA. 89:5996-6000.
19. Horrocks, W. D., J. N. Isheley, B. Holmquist, and J. S. Thompson. 1980. Structural and electronic mimics of the active site of cobalt (II)-substituted zinc metalloezymes. J. Inorg. Chem. 12:131-141.
20. 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.
21. Katre, N. V., Y. Kimura, and R. M. Stroud. 1986. Cation binding sites on the projected structure of bacteriorhodopsin. Biophys. J. 50:277-284.
22. Kobayashi, T., H. Ohtani, J. Iwai, A. Ikegami, and H. Uchiki. 1983. Effect of pH on the photoreaction cycles of bacteriorhodopsin. FEBS Lett. 162:197-200.
23. Lee, P. A., P. H. Citrin, P. Eisenberger, and B. M. Kincaid. 1981. Extended x-ray absorption fine structure: its strength and limitations as a structural tool. Rev. Mod. Phys. 53:769-806.
24. Logunov, S. L., M. A. El-Sayed, and J. K. Lanyi. 1996. Catalysis of the retinal subpicosecond process in acid purple bacteriorhodopsin and some bacteriorhodopsin mutants by chloride ions. Biophy. J. 71:1545-1553.
25. Lozier, R. H., W. Niederberger, R. A. Bogomolni, S. B. Hwang, and W. Stoeckenius. 1976. Kinetics and stoichiometry of light-induced proton release and uptake from purple membrane fragments, Halobacterium halobium cell envelopes and phospholipid vesicles containing oriented purple membrane. Biochim. Biophys. Acta. 440:545-556.
26. Marti, T., H. Otto, S. J. Rosselet, M. P. Heyn, and H. G. Khorana. 1992. Anion binding to the Schiff base of bacteriorhodopsin mutants Asp-85→Asp/Asp-212→Asn and Arg-82→Gln/Asp-85→Asn/Asp-212→Asn. J. Biol.Chem. 267:16922-16927.
27. 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.
28. Mustre de Leon, J., J. J. Rohr, S. L. Zabinsky, and R. C. Albers. 1991. Ab initial curved-wave x-ray-absorption fine structure. Phys. Rev. B. 44: 4146-4156.
29. Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233: 149-152.
30. 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.
31. Ort, D. R., and W. W. Parson. 1978. Flashed-induced volume changes of bacteriorhodopsin-containing membrane fragments and their relationship to proton movements and absorbance transients. J. Biol. Chem. 253:6158-6164.
32. 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.
33. Papadopoulos, G., N. A. Dencher, G. Zaccai, and G. Bualdt. 1990. Water molecules and exchangeable hydrogen ions at the active center of bacteriorhodopsin localized by neutron diffraction: elements of the proton pathway? J. Mol. Biol. 214:15-19.
34. 2+ binding to phosphatidylcholine. A study comparing data from optical, NMR, and infrared spectroscopies. Biophys. J. 56:551-557.
35. 3+ binding site in regenerated bacteriorhodopsin that is coordinated with the protein and the phospholipid head groups. Proc. Natl. Acad. Sci. USA. 93:14333-14337.
36. Sepulcre, F., J. Cladera, J. Garcia, M. G. Proietti, J. Torres, and E. Padros. 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.
37. Sheves, M., A. Albeck, N. Friedman, and M. Ottolenghi. 1986. Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogs. Proc. Natl. Acad. Sci. USA. 83:3262-3266.
38. Stern, E. A., Y. Ma, O. Hanske-Petitpierre, and C. E. Bouldin. 1992. Radial distribution function in x-ray-absorption fine structure. Phys. Rev. B. 46:687-694.
39. Stuart, J. A., B. W. Vought, C. Zhang, and R. R. Birge. 1995. The active site of bacteriorhodopsin. Two-photon spectroscopic evidence for a positively charged chromophore binding site mediated by calcium. Biospectroscopy. 1:9-28.
40. Sweetman, L. L., and M. A. El-Sayed. 1991. The binding site of the strongly bound europium(3+) in europium(3+)-regenerated bacteriorhodopsin. FEBS Lett. 282:436-440.
41. 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.
42. Szundi, I., and W. Stoeckenius. 1988. Purple-to-blue transition of bacteriorhodopsin in a neutral lipid environment. Biophys. J. 54:227-232.
43. Szundi, I., and W. Stoeckenius. 1989. Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface. Biophys. J. 56:369-383.
44. 2 zinc finger by a single point mutation. Proc. Natl. Acad. Sci. USA. 88:9989-9993.
45. 2+ to the two high-affinity sites of bacteriorhodopsin. J. Phys. Chem. 99:11600-11604.
46. Zhang, K., B. Chance, D. S. Auld, K. S. Larsen, and B. L. Vallee. 1992a. X-ray absorption fine structure study of the active site of zinc and cobalt carboxypeptidase A in their solution and crystalline forms. Biochemistry. 31:1159.
47. Zhang, K. E., A. Stern, F. Ellis, J. Sanders-Loehr, and A. K. Shiemke. 1988. The active site of hemerythrin as determined by x-ray absorption fine structure. Biochemistry. 27:7470-7479.
48. Zhang, K., G. Rosenbaum, and G. Bunker. 1992b. The correction of the dead time loss of the Ge detector in x-ray absorption spectroscopy. Jpn. J. Appl. Phys. 32(Suppl. 32-2):147-149.
49. Zhang, N. Y., and M. A. El-Sayed. 1993. The C-terminus and the calcium low-affinity binding sites in bacteriorhodopsin. Biochemistry. 32: 14173-14175.
50. Zhang, N. Y., M. A. El-Sayed, M. L. Bonet, J. K. Lanyi, M. Chang, B. Ni, and R. Needleman. 1993. Effects of genetic replacements of charged and hydrogen-bonding residues in the retinal pocket on calcium binding to deionized bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 90:1445-1449.
51. 2+-regenerated bacteriorhodopsin. Biophys. J. 61:1201-1206.