Journal of Photoscience

Korean Society of Photoscience (한국광과학회)
권호 표지

PROTEIN CONFORMATIONS OF OCTOPUS RHODOPSIN AND ITS DEPROTONATED PHOTOCYCLE INTERMEDIATE MONITORED BY ABSORPTION AND PROTEIN FLUORESCENCE

  • Jang, Du-Jeon (Department of Chemistry, Seoul National University) ;
  • Lee, SunBae (Department of Chemistry, Seoul National University)
  • Published : 1995.03.01
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Abstract

Picosecond time-resolved and static protein fluorescence spectra and absorption spectra of octopus rhodopsin, a photorecepting protein, are measured and compared with those of bacteriorhodopsin, a photon-induced proton pumping protein, to understand the protein conformations and functions of octopus rhodopsin and its deprotonated photocycle intermediate. The bluer and weaker absorption of retinal indicates that octopus rhodopsin is better in thermal noise suppression but less efficient in light harvesting than bacteriorhodopsin. The protein fluorescence of octopus rhodopsin shows the characteristic of Trp only and the uantum efficiency and lifetime variations may result primarily from variations in the coupling strength with the retinal. The stronger intensity by four times and larger red shift by 12 nm of fluorescence suggest that octopus rhodopsin has more open and looser structure compared with bacteriorhodopsin. Fluorescence decay profiles reveal two decay components of 300 ps (60%) and 2 ns (40%). The deprotonation of protonated Schiff's base increases the shorter decay time to 500 ps and enhances the fluorescence intensity by 20%. The fluorescence and its decay time from Trp residues near retinal are influenced more by the deprotonation. The increase of fluorescence intimates that protein structure becomes loosened and relaxed further by the deprotonation of protonated Schiff's base. The driving force of sequential changes initiated by absorption of a photon is too exhausted after the deprotonation to return the intermediate to the ground state of the begun rhodopsin form.

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References

  1. Biochim. Biophys. Acta v.1016 Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin Birge,R.
  2. Proc. Natl. Acad. Sci. USA v.76 Amino acid sequence of bacteriorhodopsin Khorana,H.G.;G.E.Gerber;W.C.Herlihy;C.P.Gray;R.J.Anderegg;K.Nihei;K.Biemann
  3. Adv. Photochem v.12 The photochemistry of rhodopsin Ottolenghi,M.
  4. J. Membr. Biol v.112 Synthetic retinals as probes for the binding site and photoreactions in rhodopsin Ottolenghi,M.;M.Sheves
  5. FEBS Lett v.148 Rhodopsin and bacteriohodopsin: structure-function relationships Ovchinnikov,Y.A.
  6. FEBS Lett v.100 The structural basis of the functioning of bacteriorhodopsin: An overview Ovchinnikov,Y.A.;N.G.Abdulaev;M.Y.Feigina;A.V.Kiselev;N.A.Lobanov
  7. Biochemistry v.33 Bacteriorhodopsin can function without a covalent linkage between retinal and protein U.Schweiger;J.Tittor;D.Oesterhelt
  8. Proc. Natl. Acad. Sci. USA v.92 Structure and function in rhodopsin: The fate of opsin formed upon the decay of light-activated metarhodopsin Ⅱ in vitro T.Sakamoto;H.G.Khorana
  9. Photochem. Photobiol v.50 Vibrational spectra of rhodopsin and bacteriorhodopsin Kitagawa,K.;A.Maeda
  10. J. Photochem. Photobiol. A v.58 Photoisomerization of rhodopsin and bacteriorhodopsin: an ab initio study Yadav,A.;R.A.Poirier
  11. Proc. Natl. Acad. Sci. USA v.90 Two light-transducing membrane proteins: bacteriorhodopsin and mammalian rhodopsin Khorana,H.G.
  12. FEBS Lett v.359 Fluorescence spectra of bacteriorhodopsin and the intermediates O and Q at room temperature H.Ohtani;Y.Tsukamoto;Y.Sakada;H.Hamaguchi
  13. Photochem. Photobiol v.45 Photoreception and phototransduction in invertebrate photoreceptors Tsuda,M.
  14. FEBS Lett v.3 Infrared studies of octopus rhodopsin: Existence of a long-lived intermediate and the states of the carboxylic group of Asp-81 in rhodopsin and its photoproducts S.Masuda;E.H.Morita;M.Tasumi;T.Iwasa;M.Tsuda
  15. Biocheim. Biophys. Acta v.545 Transient spectra of intermediates in the photolytic sequence of octopus rhodopsin Tsuda,M.
  16. Annu. Rev. Biochem v.51 Bacteriorhodopsin and related pigment of halobacteria Stoeckenius,W.;R.A.Bogomolni
  17. Biophys. J v.15 Bacteriorhodopsin, a light-driven proton pump in Halabacterium halobium Lozier,R.H.;R.A.Bogomolini;W.Stoeckenius
  18. Biochemistry v.32 Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185→Phe: Evidence for an equilibrium between $bR_{570}$ and on O-like species Sonar,S.;M.P.Krebs;H.G.Khorana;K.J.Rothschild
  19. Biophys. J v.64 Deriving the intermediate spectra and photocycle kinetics from time-resolved difference spectra of bacteriorhodopsin Zimanyi,L.;J.K.Lanyi
  20. Acc. Chem. Res v.13 Purple membrane of halobacteria: a new light-energy converter Stoeckenius,W.
  21. Ann. Rev. Biochem v.54 Time-resolved fluorescence of proteins Beechem,J.M.;L.Brand
  22. Photochem. Photobiol v.48 Effects of metal cations, retinal, and the photocycle on the tryptophan emission in bacteriorhodopsin Jang,D.J.;T.C.Corcoran;M.A.El-Sayed
  23. Proc. Natl. Acad. Sci. USA v.86 Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations Jang,D.J.;M.A.El-Sayed
  24. Biophys. J v.57 decay of the tryptophan fluorescence anisotropy in bacteriorhodopsin and its modified forms Van den Berg,R.;D.J.Jang;M.A.El-Sayed
  25. FEBS Lett v.284 The use of tryptophan mutants in identifying the 296nm transient absorbing species during the photocycle of bacteriorhodopsin Wu,S.;D.J.Jang;M.A.El-Sayed;T.Marti;T.Mogi;H.Gobind
  26. Photochem. Photobiol v.36 Time-resolved fluorometry of bacteriorhodopsin Sherman,W.V.
  27. Photochem. Photobiol v.42 Alkaline quenching of bacteriorhodopsin tryptophanyl fluorescence: evidence for aqueous acessibility or a hydrogen bonded chain Palmer,P.L.;W.V.Sherman
  28. Biochemistry v.20 Photochemist'y and fluorescence of bacteriorhodopsin excited in its 280nm absorption band Kalisky,O.;J.Feitelson;M.Ottolenghi
  29. Biophys. J v.53 Primary processes in photolysis of octopus rhodopsin Ohtani,H.;T.Kobayashi;M.Tsuda;T.G.Ebrey
  30. Methods Enzymol v.31 Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Oesterhelt,D.;W.Stoeckenius
  31. Prep. Biochem v.5 Improved isolation procedures for the purple membrane of Halobacterium halobium Becher,B.M.;J.Y.Cassim
  32. J. Photochem. Photobiol. A: Chem v.80 A study on the photophysical properties of anthracene in zeolite Park,J.;W.K.Kang;R.Ryoo;K.H.Jung;D.J.Jang
  33. J. Am. Chem. Soc v.102 An external point-charge model for bacteriorhodopsin to account for its purple color Nakanishi,K.;V.Balogh-Nair;M.Arnaboldi;K.Tsujimoto;B.Honig
  34. Biochemistry v.31 Rhodopsin: Structure, Function and Genetics Nathans,J.
  35. Biophys. J v.60 Red shift of the purple membrane absorption band and the deprotonatin of tyrosine residues at high pH Balashov,S.;R.Govindjee;T.Ebrey
  36. Biophys. J v.64 The unusual pK a of the rhodopsin chromophore: Is this how Nature minimizes photoreceptor noise? Birge,R.
  37. Photochemistry of proteins and nucleic acids McLaren,A.;D.Shugar
  38. Physical Principle and Techniques of Protein Chemistry Ultraviolet absorption Donovan,J.W.;S.J.Leach(ed.)
  39. Modern Molecular Photochemistry Turro,N.J.