메뉴 건너뛰기




Volumn 328, Issue 2, 2003, Pages 439-450

Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2′ intermediates of the photocycle

Author keywords

Bacteriorhodopsin; Ion pump; Retinal; Transport mechanism; X ray diffraction

Indexed keywords

BACTERIORHODOPSIN; PROTON; SCHIFF BASE;

EID: 0037466289     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00263-8     Document Type: Article
Times cited : (146)

References (44)
  • 1
  • 2
    • 0034499002 scopus 로고    scopus 로고
    • Molecular mechanism of ion transport in bacteriorhodopsin: Insights from crystallographic, spectroscopic and mutational studies
    • Lanyi J.K. Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic and mutational studies. J. Phys. Chem. B. 104:2000;11441-11448.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11441-11448
    • Lanyi, J.K.1
  • 3
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi J.K., Váró G. The photocycles of bacteriorhodopsin. Israel J. Chem. 35:1995;365-386.
    • (1995) Israel J. Chem. , vol.35 , pp. 365-386
    • Lanyi, J.K.1    Váró, G.2
  • 5
    • 85005500629 scopus 로고
    • Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin
    • Maeda A. Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin. Israel J. Chem. 35:1995;387-400.
    • (1995) Israel J. Chem. , vol.35 , pp. 387-400
    • Maeda, A.1
  • 6
    • 0000580157 scopus 로고    scopus 로고
    • Monitoring fast reactions of slow cycling systems with time-resolved FTIR spectroscopy
    • Rodig C., Siebert F. Monitoring fast reactions of slow cycling systems with time-resolved FTIR spectroscopy. Vib. Spectrosc. 19:1999;271-276.
    • (1999) Vib. Spectrosc. , vol.19 , pp. 271-276
    • Rodig, C.1    Siebert, F.2
  • 7
    • 0032877232 scopus 로고    scopus 로고
    • Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy
    • Gerwert K. Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy. Biol. Chem. 380:1999;931-935.
    • (1999) Biol. Chem. , vol.380 , pp. 931-935
    • Gerwert, K.1
  • 8
    • 0036089699 scopus 로고    scopus 로고
    • Magnetic resonance studies of the bacteriorhodopsin pump cycle
    • Herzfeld J., Lansing J.C. Magnetic resonance studies of the bacteriorhodopsin pump cycle. Annu. Rev. Biomol. Struct. 31:2002;73-95.
    • (2002) Annu. Rev. Biomol. Struct. , vol.31 , pp. 73-95
    • Herzfeld, J.1    Lansing, J.C.2
  • 9
    • 0031829172 scopus 로고    scopus 로고
    • Lipidic cubic phases: New matrices for the three-dimensional crystallization of membrane proteins
    • Rummel G., Hardmeyer A., Widmer C., Chiu M.L., Nollert P., Locher K.P., et al. Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane proteins. J. Struct. Biol. 121:1998;82-91.
    • (1998) J. Struct. Biol. , vol.121 , pp. 82-91
    • Rummel, G.1    Hardmeyer, A.2    Widmer, C.3    Chiu, M.L.4    Nollert, P.5    Locher, K.P.6
  • 10
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., Pebay-Peyroula E.H. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Structure. 7:1999;909-917.
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.H.7
  • 12
    • 0036971196 scopus 로고    scopus 로고
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: Conservation of free energy after photoisomerization of the retinal
    • Schobert B., Cupp-Vickery J., Hornak V., Smith S.O., Lanyi J.K. Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. J. Mol. Biol. 321:2002;715-726.
    • (2002) J. Mol. Biol. , vol.321 , pp. 715-726
    • Schobert, B.1    Cupp-Vickery, J.2    Hornak, V.3    Smith, S.O.4    Lanyi, J.K.5
  • 13
    • 0033592726 scopus 로고    scopus 로고
    • High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle
    • Edman K., Nollert P., Royant A., Belrhali H., Pebay-Peyroula E., Hajdu J., et al. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature. 401:1999;822-826.
    • (1999) Nature , vol.401 , pp. 822-826
    • Edman, K.1    Nollert, P.2    Royant, A.3    Belrhali, H.4    Pebay-Peyroula, E.5    Hajdu, J.6
  • 14
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., Neutze R. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature. 406:2000;645-648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E.M.5    Neutze, R.6
  • 15
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in the M photointermediate of bacteriorhodopsin at 2 Å resolution
    • Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., Lanyi J.K. Structural changes in the M photointermediate of bacteriorhodopsin at 2 Å resolution. Science. 286:1999;255-260.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 17
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass H.J., Buldt G., Gessenich R., Hehn D., Neff D., Schlesinger R., et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature. 406:2000;649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6
  • 18
  • 19
    • 0036968773 scopus 로고    scopus 로고
    • Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: The switch in the bacteriorhodopsin photocycle
    • Lanyi J.K., Schobert B. Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle. J. Mol. Biol. 321:2002;727-737.
    • (2002) J. Mol. Biol. , vol.321 , pp. 727-737
    • Lanyi, J.K.1    Schobert, B.2
  • 20
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck J. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 19:2000;2152-2160.
    • (2000) EMBO J. , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 21
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by Bacteriorhodopsin
    • Subramaniam S., Henderson R. Molecular mechanism of vectorial proton translocation by Bacteriorhodopsin. Nature. 406:2000;653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 23
    • 0035345448 scopus 로고    scopus 로고
    • Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
    • Balashov S.P., Ebrey T.G. Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures. Photochem. Photobiol. 73:2001;453-462.
    • (2001) Photochem. Photobiol. , vol.73 , pp. 453-462
    • Balashov, S.P.1    Ebrey, T.G.2
  • 24
    • 0035498348 scopus 로고    scopus 로고
    • Internal water molecules as mobile polar groups for light-induced proton translocation in bacteriorhodopsin and rhodopsin as studied by difference FTIR
    • Maeda A. Internal water molecules as mobile polar groups for light-induced proton translocation in bacteriorhodopsin and rhodopsin as studied by difference FTIR. Biochemistry (Moscow). 66:2001;1256-1268.
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 1256-1268
    • Maeda, A.1
  • 25
    • 0034734251 scopus 로고    scopus 로고
    • Lipidic cubic phase crystallization of bacteriorhodopsin and cryotrapping of intermediates: Towards resolving a revolving photocycle
    • Pebay-Peyroula E., Neutze R., Landau E.M. Lipidic cubic phase crystallization of bacteriorhodopsin and cryotrapping of intermediates: towards resolving a revolving photocycle. Biochim. Biophys. Acta. 1460:2000;119-132.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 119-132
    • Pebay-Peyroula, E.1    Neutze, R.2    Landau, E.M.3
  • 26
    • 0035790044 scopus 로고    scopus 로고
    • Spectroscopic characterization of bacteriorhodopsin's L-intermediate in 3D crystals cooled to 170 K
    • Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., Neutze R. Spectroscopic characterization of bacteriorhodopsin's L-intermediate in 3D crystals cooled to 170 K. Photochem. Photobiol. 74:2001;794-804.
    • (2001) Photochem. Photobiol. , vol.74 , pp. 794-804
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E.M.5    Neutze, R.6
  • 27
    • 0020008581 scopus 로고
    • Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore
    • Braiman M., Mathies R.A. Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore. Proc. Natl Acad. Sci. USA. 79:1982;403-407.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 403-407
    • Braiman, M.1    Mathies, R.A.2
  • 28
    • 84989669798 scopus 로고
    • Fourier transform infrared spectral studies of the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates K and L
    • Maeda A., Sasaki J., Pfefferlé J.-M., Shichida Y., Yoshizawa T. Fourier transform infrared spectral studies of the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates K and L. Photochem. Photobiol. 54:1991;911-921.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 911-921
    • Maeda, A.1    Sasaki, J.2    Pfefferlé, J.-M.3    Shichida, Y.4    Yoshizawa, T.5
  • 31
    • 0001385068 scopus 로고
    • Photoisomerization in bacteriorhodopsin studied by FTIR, linear dichroism, and photoselection experiments combined with quantum chemical theoretical calculations
    • Fahmy K., Siebert F., Grossjean M.F., Tavan P. Photoisomerization in bacteriorhodopsin studied by FTIR, linear dichroism, and photoselection experiments combined with quantum chemical theoretical calculations. J. Mol. Struct. 214:1989;257-288.
    • (1989) J. Mol. Struct. , vol.214 , pp. 257-288
    • Fahmy, K.1    Siebert, F.2    Grossjean, M.F.3    Tavan, P.4
  • 33
    • 0037133147 scopus 로고    scopus 로고
    • Tryptophan interactions in bacteriorhodopsin: A heteronuclear solid-state NMR study
    • Petkova A.T., Hatanaka M., Jaroniec C.P., Hu J.G., Belenky M., Verhoeven M., et al. Tryptophan interactions in bacteriorhodopsin: a heteronuclear solid-state NMR study. Biochemistry. 41:2002;2429-2437.
    • (2002) Biochemistry , vol.41 , pp. 2429-2437
    • Petkova, A.T.1    Hatanaka, M.2    Jaroniec, C.P.3    Hu, J.G.4    Belenky, M.5    Verhoeven, M.6
  • 34
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró G., Lanyi J.K. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry. 30:1991;5016-5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Váró, G.1    Lanyi, J.K.2
  • 36
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov S.P., Imasheva E.S., Govindjee R., Ebrey T.G. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70:1996;473-481.
    • (1996) Biophys. J. , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 37
    • 0029665673 scopus 로고    scopus 로고
    • a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • a's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:1996;4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 38
    • 0026703071 scopus 로고
    • N intermediate with unprotonated Schiff base but N-like protein structure
    • N intermediate with unprotonated Schiff base but N-like protein structure. J. Biol. Chem. 267:1992;20782-20786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20782-20786
    • Sasaki, J.1    Shichida, Y.2    Lanyi, J.K.3    Maeda, A.4
  • 39
    • 0034734227 scopus 로고    scopus 로고
    • NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: Evidence for an "electrostatic steering" mechanism
    • Herzfeld J., Tounge B. NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: evidence for an "electrostatic steering" mechanism. Biochim. Biophys. Acta. 1460:2000;95-105.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 95-105
    • Herzfeld, J.1    Tounge, B.2
  • 40
    • 0025871066 scopus 로고
    • Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle
    • Váró G., Lanyi J.K. Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biochemistry. 30:1991;5008-5015.
    • (1991) Biochemistry , vol.30 , pp. 5008-5015
    • Váró, G.1    Lanyi, J.K.2
  • 41
    • 0026452122 scopus 로고
    • Interrelations of M-intermediates in bacteriorhodopsin photocycle
    • Drachev L.A., Kaulen A.D., Komrakov Y. Interrelations of M-intermediates in bacteriorhodopsin photocycle. FEBS Letters. 313:1992;248-250.
    • (1992) FEBS Letters , vol.313 , pp. 248-250
    • Drachev, L.A.1    Kaulen, A.D.2    Komrakov, Y.3
  • 42
    • 0034620606 scopus 로고    scopus 로고
    • Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle
    • Brown L.S., Needleman R., Lanyi J.K. Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle. Biochemistry. 39:2000;938-945.
    • (2000) Biochemistry , vol.39 , pp. 938-945
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 43
    • 0002452464 scopus 로고
    • SCALEPACK data collection and processing
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington, UK: SERC Daresbury Lab
    • Otwinowski Z. SCALEPACK data collection and processing. Sawyer L., Isaacs N., Bailey S. Data Collection and Processing. 1993;UK SERC Daresbury Lab, Warrington, UK.
    • (1993) Data Collection and Processing
    • Otwinowski, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.