메뉴 건너뛰기




Volumn 91, Issue 1, 2006, Pages 255-262

First steps of retinal photoisomerization in proteorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN; PROTEORHODOPSIN; PROTON PUMP; UNCLASSIFIED DRUG;

EID: 33745759633     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.074690     Document Type: Article
Times cited : (71)

References (43)
  • 4
    • 0038636606 scopus 로고    scopus 로고
    • The photochemical reaction cycle of proteorhodopsin at low pH
    • Lakatos, M., J. K. Lanyi, J. Szakacs, and G. Varo. 2003. The photochemical reaction cycle of proteorhodopsin at low pH. Biophys. J. 84:3252-3256.
    • (2003) Biophys. J. , vol.84 , pp. 3252-3256
    • Lakatos, M.1    Lanyi, J.K.2    Szakacs, J.3    Varo, G.4
  • 7
    • 0038390509 scopus 로고    scopus 로고
    • Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic
    • Dioumaev, A. K., J. M. Wang, Z. Balint, G. Varo, and J. K. Lanyi. 2003. Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic. Biochemistry. 42:6582-6587.
    • (2003) Biochemistry , vol.42 , pp. 6582-6587
    • Dioumaev, A.K.1    Wang, J.M.2    Balint, Z.3    Varo, G.4    Lanyi, J.K.5
  • 8
    • 0037304406 scopus 로고    scopus 로고
    • Characterization of the photochemical reaction cycle of proteorhodopsin
    • Varo, G., L. S. Brown, M. Lakatos, and J. K. Lanyi. 2003. Characterization of the photochemical reaction cycle of proteorhodopsin. Biophys. J. 84:1202-1207.
    • (2003) Biophys. J. , vol.84 , pp. 1202-1207
    • Varo, G.1    Brown, L.S.2    Lakatos, M.3    Lanyi, J.K.4
  • 9
    • 0042233486 scopus 로고    scopus 로고
    • Resonance Raman characterization of proteorhodopsin's chromophore environment
    • Krebs, R. A., D. Dunmire, R. Partha, and M. S. Braiman. 2003. Resonance Raman characterization of proteorhodopsin's chromophore environment. J. Phys. Chem. B. 107:7877-7883.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 7877-7883
    • Krebs, R.A.1    Dunmire, D.2    Partha, R.3    Braiman, M.S.4
  • 10
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saito, 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.
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saito, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 11
    • 0030808219 scopus 로고    scopus 로고
    • Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    • Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry. 36:8671-8676.
    • (1997) Biochemistry , vol.36 , pp. 8671-8676
    • Balashov, S.P.1    Imasheva, E.S.2    Ebrey, T.G.3    Chen, N.4    Menick, D.R.5    Crouch, R.K.6
  • 12
    • 0028864699 scopus 로고
    • Glutamic-acid-204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • 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.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 13
    • 3242801403 scopus 로고    scopus 로고
    • Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells
    • Sineshchekov, O. A., and J. L. Spudich. 2004. Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells. Photochem. Photobiol. Sci. 3:548-554.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 548-554
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 14
    • 3142779894 scopus 로고    scopus 로고
    • Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction
    • Bergo, V., J. J. Amsden, E. N. Spudich, J. L. Spudich, and K. J. Rothschild. 2004. Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction. Biochemistry. 43: 9075-9083.
    • (2004) Biochemistry , vol.43 , pp. 9075-9083
    • Bergo, V.1    Amsden, J.J.2    Spudich, E.N.3    Spudich, J.L.4    Rothschild, K.J.5
  • 15
    • 23844528739 scopus 로고    scopus 로고
    • Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp-227
    • Imasheva, E. S., K. Shimono, S. P. Balashov, J. M. Wang, U. Zadok, M. Sheves, N. Kamo, and J. K. Lanyi. 2005. Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp-227. Biochemistry. 44:10828-10838.
    • (2005) Biochemistry , vol.44 , pp. 10828-10838
    • Imasheva, E.S.1    Shimono, K.2    Balashov, S.P.3    Wang, J.M.4    Zadok, U.5    Sheves, M.6    Kamo, N.7    Lanyi, J.K.8
  • 17
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts, U., J. Tittor, and D. Oesterhelt. 1999. Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu. Rev. Biophys. Biomol. Struct. 28:367-399.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 18
    • 0034499002 scopus 로고    scopus 로고
    • Molecular mechanism of ion transport in bacteriorhodopsin: Insights from crystallographic, spectroscopic, kinetic, and mutational studies
    • Lanyi, J. K. 2000. Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic, and mutational studies. J. Phys. Chem. B. 104:11441-11448.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11441-11448
    • Lanyi, J.K.1
  • 19
    • 0032475417 scopus 로고    scopus 로고
    • Primary step in bacteriorhodopsin photosynthesis: Bond stretch rather than angle twist of its retinal excited-state structure
    • Song, L., and M. A. El-Sayed. 1998. Primary step in bacteriorhodopsin photosynthesis: bond stretch rather than angle twist of its retinal excited-state structure. J. Am. Chem. Soc. 120:8889-8890.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8889-8890
    • Song, L.1    El-Sayed, M.A.2
  • 20
    • 0030794947 scopus 로고    scopus 로고
    • The C5H6NH21 protonated Shiff base: An ab initio minimal model for retinal photoisomerization
    • Garavelli, M., P. Celani, F. Bernardi, M. A. Robb, and M. Olivucci. 1997. The C5H6NH21 protonated Shiff base: an ab initio minimal model for retinal photoisomerization. J. Am. Chem. Soc. 119:6891-6901.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6891-6901
    • Garavelli, M.1    Celani, P.2    Bernardi, F.3    Robb, M.A.4    Olivucci, M.5
  • 22
    • 0037123226 scopus 로고    scopus 로고
    • Reaction path analysis of the "tunable" photoisomerization selectivity of free and locked retinal chromophores
    • De Vico, L., C. S. Page, M. Garavelli, F. Bernardi, R. Basosi, and M. Olivucci. 2002. Reaction path analysis of the "tunable" photoisomerization selectivity of free and locked retinal chromophores. J. Am. Chem. Soc. 124:4124-4134.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4124-4134
    • De Vico, L.1    Page, C.S.2    Garavelli, M.3    Bernardi, F.4    Basosi, R.5    Olivucci, M.6
  • 23
    • 14744300709 scopus 로고    scopus 로고
    • Photoisomerization mechanism of 11-cis-locked artificial retinal chromophores: Acceleration and primary photoproduct assignment
    • De Vico, L., M. Garavelli, F. Bernardi, and M. Olivucci. 2005. Photoisomerization mechanism of 11-cis-locked artificial retinal chromophores: Acceleration and primary photoproduct assignment. J. Am. Chem. Soc. 127:2433-2442.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2433-2442
    • De Vico, L.1    Garavelli, M.2    Bernardi, F.3    Olivucci, M.4
  • 24
    • 18244373415 scopus 로고    scopus 로고
    • The retinal chromophore/chloride ion pair: Structure of the photo isomerization path and interplay of charge transfer and covalent states
    • Cembran, A., F. Bernardi, M. Olivucci, and M. Garavelli. 2005. The retinal chromophore/chloride ion pair: structure of the photo isomerization path and interplay of charge transfer and covalent states. Proc. Natl. Acad. Sci. USA. 102:6255-6260.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6255-6260
    • Cembran, A.1    Bernardi, F.2    Olivucci, M.3    Garavelli, M.4
  • 25
    • 1642407639 scopus 로고    scopus 로고
    • On the mechanism of the cis-trans isomerization in the lowest electronic states of azobenzene: S-0, S-1, and T-1
    • Cembran, A., F. Bernardi, M. Garavelli, L. Gagliardi, and G. Orlandi. 2004. On the mechanism of the cis-trans isomerization in the lowest electronic states of azobenzene: S-0, S-1, and T-1. J. Am. Chem. Soc. 126:3234-3243.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3234-3243
    • Cembran, A.1    Bernardi, F.2    Garavelli, M.3    Gagliardi, L.4    Orlandi, G.5
  • 26
    • 10444237332 scopus 로고    scopus 로고
    • Counterion controlled photoisomerization of retinal chromophore models: A computational investigation
    • Cembran, A., F. Bernardi, M. Olivucci, and M. Garavelli. 2004. Counterion controlled photoisomerization of retinal chromophore models: a computational investigation. J. Am. Chem. Soc. 126:16018-16037.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16018-16037
    • Cembran, A.1    Bernardi, F.2    Olivucci, M.3    Garavelli, M.4
  • 27
    • 2442646472 scopus 로고    scopus 로고
    • A theoretical study of the lowest electronic states of azobenzene: The role of torsion coordinate in the cis-trans photoisomerization
    • Gagliardi, L., G. Orlandi, F. Bernardi, A. Cembran, and M. Garavelli. 2004. A theoretical study of the lowest electronic states of azobenzene: the role of torsion coordinate in the cis-trans photoisomerization. Theor. Chem. Acc. 111:363-372.
    • (2004) Theor. Chem. Acc. , vol.111 , pp. 363-372
    • Gagliardi, L.1    Orlandi, G.2    Bernardi, F.3    Cembran, A.4    Garavelli, M.5
  • 28
    • 23844453429 scopus 로고    scopus 로고
    • Structure, spectroscopy, and spectral tuning of the gas-phase retinal chromophore: The beta-ionone "handle" and alkyl group effect
    • Cembran, A., R. Gonzalez-Luque, P. Altoe, M. Merchan, F. Bernardi, M. Olivucci, and M. Garavelli. 2005. Structure, spectroscopy, and spectral tuning of the gas-phase retinal chromophore: the beta-ionone "handle" and alkyl group effect. J. Phys. Chem. A. 109:6597-6605.
    • (2005) J. Phys. Chem. A , vol.109 , pp. 6597-6605
    • Cembran, A.1    Gonzalez-Luque, R.2    Altoe, P.3    Merchan, M.4    Bernardi, F.5    Olivucci, M.6    Garavelli, M.7
  • 30
    • 36849126497 scopus 로고
    • Relationship between absorption intensity and fluorescence lifetime of molecules
    • Strickler, S. J., and R. A. Berg. 1962. Relationship between absorption intensity and fluorescence lifetime of molecules. J. Chem. Phys. 37:814-820.
    • (1962) J. Chem. Phys. , vol.37 , pp. 814-820
    • Strickler, S.J.1    Berg, R.A.2
  • 31
    • 33748878838 scopus 로고    scopus 로고
    • Spontaneous emission study of the femtosecond isomerization dynamics of rhodopsin
    • Kochendoerfer, G. G., and R. A. Mathies. 1996. Spontaneous emission study of the femtosecond isomerization dynamics of rhodopsin. J. Phys. Chem. 100:14526-14532.
    • (1996) J. Phys. Chem. , vol.100 , pp. 14526-14532
    • Kochendoerfer, G.G.1    Mathies, R.A.2
  • 32
    • 5344280469 scopus 로고    scopus 로고
    • Sub-20-fs pulses tunable across the visible from a blue-pumped single-pass noncollinear parametric converter
    • Wilhelm, T., J. Piel, and E. Riedle. 1997. Sub-20-fs pulses tunable across the visible from a blue-pumped single-pass noncollinear parametric converter. Opt. Lett. 22:1494-1496.
    • (1997) Opt. Lett. , vol.22 , pp. 1494-1496
    • Wilhelm, T.1    Piel, J.2    Riedle, E.3
  • 33
    • 0035879594 scopus 로고    scopus 로고
    • Noncollinear optical parametric amplifiers with output parameters improved by the application of a white light continuum generated in CaF2
    • Huber, R., H. Satzger, W. Zinth, and J. Wachtveitl. 2001. Noncollinear optical parametric amplifiers with output parameters improved by the application of a white light continuum generated in CaF2. Opt. Commun. 194:443-448.
    • (2001) Opt. Commun. , vol.194 , pp. 443-448
    • Huber, R.1    Satzger, H.2    Zinth, W.3    Wachtveitl, J.4
  • 34
    • 0041879991 scopus 로고    scopus 로고
    • A broadband Kerr shutter for femtosecond fluorescence spectroscopy
    • Schmidt, B., S. Laimgruber, W. Zinth, and P. Gilch. 2003. A broadband Kerr shutter for femtosecond fluorescence spectroscopy. Appl. Phys. B-Lasers O. 76:809-814.
    • (2003) Appl. Phys. B-Lasers O , vol.76 , pp. 809-814
    • Schmidt, B.1    Laimgruber, S.2    Zinth, W.3    Gilch, P.4
  • 35
    • 11144292071 scopus 로고    scopus 로고
    • Excited-state dynamics of bacteriorhodopsin probed by broadband femtosecond fluorescence spectroscopy
    • Schmidt, B., C. Sobotta, B. Heinz, S. Laimgruber, M. Braun, and P. Gilch. 2005. Excited-state dynamics of bacteriorhodopsin probed by broadband femtosecond fluorescence spectroscopy. Biochim. Biophys. Acta. 1706:165-173.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 165-173
    • Schmidt, B.1    Sobotta, C.2    Heinz, B.3    Laimgruber, S.4    Braun, M.5    Gilch, P.6
  • 36
    • 1042288283 scopus 로고    scopus 로고
    • Selectivity of retinal photoisomerization in proteorhodopsin is controlled by aspartic acid 227
    • Imasheva, E. S., S. P. Balashov, J. M. Wang, A. K. Dioumaev, and J. K. Lanyi. 2004. Selectivity of retinal photoisomerization in proteorhodopsin is controlled by aspartic acid 227. Biochemistry. 43:1648-1655.
    • (2004) Biochemistry , vol.43 , pp. 1648-1655
    • Imasheva, E.S.1    Balashov, S.P.2    Wang, J.M.3    Dioumaev, A.K.4    Lanyi, J.K.5
  • 37
    • 0037008526 scopus 로고    scopus 로고
    • Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization
    • Herbst, J., K. Heyne, and R. Diller. 2002. Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization. Science. 297:822-825.
    • (2002) Science , vol.297 , pp. 822-825
    • Herbst, J.1    Heyne, K.2    Diller, R.3
  • 38
    • 3042598390 scopus 로고    scopus 로고
    • Femtosecond primary events in bacteriorhodopsin and its retinal modified analogs: Revision of commonly accepted interpretation of electronic spectra of transient intermediates in the bacteriorhodopsin photocycle
    • Abramczyk, H. 2004. Femtosecond primary events in bacteriorhodopsin and its retinal modified analogs: revision of commonly accepted interpretation of electronic spectra of transient intermediates in the bacteriorhodopsin photocycle. J. Chem. Phys. 120:11120-11132.
    • (2004) J. Chem. Phys. , vol.120 , pp. 11120-11132
    • Abramczyk, H.1
  • 40
    • 0027303125 scopus 로고
    • Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis
    • Song, L., M. A. El-Sayed, and J. K. Lanyi. 1993. Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis. Science. 261:891-894.
    • (1993) Science , vol.261 , pp. 891-894
    • Song, L.1    El-Sayed, M.A.2    Lanyi, J.K.3
  • 42
    • 23244431748 scopus 로고    scopus 로고
    • Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin
    • Schenkl, S., F. van Mourik, G. van der Zwan, S. Haacke, and M. Chergui. 2005. Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin. Science. 309:917-920.
    • (2005) Science , vol.309 , pp. 917-920
    • Schenkl, S.1    Van Mourik, F.2    Van Der Zwan, G.3    Haacke, S.4    Chergui, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.