메뉴 건너뛰기




Volumn 65, Issue 6, 1997, Pages 1039-1044

Charge Movements in the 13-cis Photocycles of the Bacteriorhodopsin Mutants R82K and R82Q

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; DEUTERIUM OXIDE;

EID: 0031159009     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1997.tb07966.x     Document Type: Article
Times cited : (3)

References (18)
  • 1
    • 0347372148 scopus 로고
    • Isomeric composition of bacteriorhodopsin under different environmental light conditions
    • Sperling, W., C. N. Rafferty, K.-D. Kohl and N. A. Dencher (1978) Isomeric composition of bacteriorhodopsin under different environmental light conditions. FEBS Lett. 97, 129-132.
    • (1978) FEBS Lett. , vol.97 , pp. 129-132
    • Sperling, W.1    Rafferty, C.N.2    Kohl, K.-D.3    Dencher, N.A.4
  • 2
    • 0024744044 scopus 로고
    • Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy
    • Hofrichter, J., E. R. Henry and R. H. Lozier (1989) Photocycles of bacteriorhodopsin in light-and dark-adapted purple membrane studied by time-resolved absorption spectroscopy. Biophys. J. 56, 693-706.
    • (1989) Biophys. J. , vol.56 , pp. 693-706
    • Hofrichter, J.1    Henry, E.R.2    Lozier, R.H.3
  • 3
    • 0028136025 scopus 로고
    • Combined optical and photoelectric study of the photocycle of 13-cis bacterio-rhodopsin
    • Gergely, C., C. Ganea and G. Váró (1994) Combined optical and photoelectric study of the photocycle of 13-cis bacterio-rhodopsin. Biophys. J. 67, 855-861.
    • (1994) Biophys. J. , vol.67 , pp. 855-861
    • Gergely, C.1    Ganea, C.2    Váró, G.3
  • 4
    • 24544443225 scopus 로고
    • Molecular dynamics study of the 13-cis photocycle of bacteriorhodopsin
    • Logunov, I., W. Humphrey, K. Schulten and M. Sheves (1994) Molecular dynamics study of the 13-cis photocycle of bacteriorhodopsin. Biophys. J. 66, A44.
    • (1994) Biophys. J. , vol.66
    • Logunov, I.1    Humphrey, W.2    Schulten, K.3    Sheves, M.4
  • 5
    • 0027453982 scopus 로고
    • Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle
    • Balashov, S. P., R. Govindjee, M. Kono, E. Imasheva, E. Lukashev, T. G. Ebrey, R. K. Crouch, D. R. Menick and Y. Feng (1993) Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle. Biochemistry 32, 10331-10343.
    • (1993) Biochemistry , vol.32 , pp. 10331-10343
    • Balashov, S.P.1    Govindjee, R.2    Kono, M.3    Imasheva, E.4    Lukashev, E.5    Ebrey, T.G.6    Crouch, R.K.7    Menick, D.R.8    Feng, Y.9
  • 7
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov, S. P., E. S. Imasheva, R. Govindjee and T. G. Ebrey (1996) Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70, 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
  • 8
    • 0012966233 scopus 로고
    • Photocurrents of dark-adapted bacteriorhodopsin on black lipid membranes
    • Fahr, A. and E. Bamberg (1982) Photocurrents of dark-adapted bacteriorhodopsin on black lipid membranes. FEBS Lett. 140, 251-253.
    • (1982) FEBS Lett. , vol.140 , pp. 251-253
    • Fahr, A.1    Bamberg, E.2
  • 9
    • 0021983430 scopus 로고
    • Time-resolved photoelectric and absorption signals from oriented purple membranes immobilized in gel
    • Dér, A., P. Harigittai and J. Simon (1985) Time-resolved photoelectric and absorption signals from oriented purple membranes immobilized in gel. J. Biochem. Biophys. Methods 10, 259-300.
    • (1985) J. Biochem. Biophys. Methods , vol.10 , pp. 259-300
    • Dér, A.1    Harigittai, P.2    Simon, J.3
  • 10
    • 0025308625 scopus 로고
    • Light-induced currents from oriented purple membrane. I. Correlation of the microsecond component (B2) with the L-M photocycle transition
    • Liu, S. Y. (1990) Light-induced currents from oriented purple membrane. I. Correlation of the microsecond component (B2) with the L-M photocycle transition. Biophys. J. 57, 943-950.
    • (1990) Biophys. J. , vol.57 , pp. 943-950
    • Liu, S.Y.1
  • 11
    • 0025034111 scopus 로고
    • Quantum efficiency of the photochemical cycle of bacteriorhodopsin
    • Govindjee, R., S. P. Balashov and T. G. Ebrey (1990) Quantum efficiency of the photochemical cycle of bacteriorhodopsin. Biophys. J. 58, 597-608.
    • (1990) Biophys. J. , vol.58 , pp. 597-608
    • Govindjee, R.1    Balashov, S.P.2    Ebrey, T.G.3
  • 12
    • 0017389861 scopus 로고
    • On the photocycle and light adaptation of dark-adapted bacteriorhodopsin
    • Kalisky, O., C. R. Goldschmidt and M. Ottolenghi (1977) On the photocycle and light adaptation of dark-adapted bacteriorhodopsin. Biophys. J. 19, 185-189.
    • (1977) Biophys. J. , vol.19 , pp. 185-189
    • Kalisky, O.1    Goldschmidt, C.R.2    Ottolenghi, M.3
  • 13
    • 0025442408 scopus 로고
    • Photoelectric measurements of purple membranes
    • Trissl, H.-W. (1990) Photoelectric measurements of purple membranes. Photochem. Photobiol. 51, 793-818.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 793-818
    • Trissl, H.-W.1
  • 14
    • 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, 4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 15
    • 0018640375 scopus 로고
    • Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
    • Mowery, P. C., R. H. Lozier, Q. Chae, Y.-W. Tseng, M. Taylor and W. Stoeckenius (1979) Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry 18, 4100-4107.
    • (1979) Biochemistry , vol.18 , pp. 4100-4107
    • Mowery, P.C.1    Lozier, R.H.2    Chae, Q.3    Tseng, Y.-W.4    Taylor, M.5    Stoeckenius, W.6
  • 16
    • 0025157075 scopus 로고
    • 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
    • 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. Acacl. Sci. USA 87, 1013-1017.
    • (1990) Proc. Natl. Acacl. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.