메뉴 건너뛰기




Volumn 66, Issue 6, 1997, Pages 755-763

Nano- and Microsecond Time-Resolved FTIR Spectroscopy of the Halorhodopsin Photocycle

Author keywords

[No Author keywords available]

Indexed keywords

MUS;

EID: 0031306645     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1997.tb03220.x     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 0345845436 scopus 로고
    • Progress in halorhodopsin
    • Edited by Y. A. Ovchinnikov, VNU Science Press, Utrecht
    • Hegemann, P., J. Tittor, A. Blanck and D. Oesterhelt (1987) Progress in halorhodopsin. In Retinal Proteins (Edited by Y. A. Ovchinnikov), pp. 333-352. VNU Science Press, Utrecht.
    • (1987) Retinal Proteins , pp. 333-352
    • Hegemann, P.1    Tittor, J.2    Blanck, A.3    Oesterhelt, D.4
  • 2
    • 0025311055 scopus 로고
    • Anion binding to the chloride pump, halorhodopsin, and its implications for the transport mechanism
    • Lanyi, J. K., A. Duschl, G. Váró and L. Zimanyi (1990) Anion binding to the chloride pump, halorhodopsin, and its implications for the transport mechanism. FEBS Lett. 265, 1-6.
    • (1990) FEBS Lett. , vol.265 , pp. 1-6
    • Lanyi, J.K.1    Duschl, A.2    Váró, G.3    Zimanyi, L.4
  • 3
    • 85005560634 scopus 로고
    • Structure and function of halorhodopsin
    • Oesterhelt, D. (1995) Structure and function of halorhodopsin. Isr. J. Chem. 35, 475-494.
    • (1995) Isr. J. Chem. , vol.35 , pp. 475-494
    • Oesterhelt, D.1
  • 4
    • 0027401509 scopus 로고
    • Homologous overexpression of a light-driven anion pump in an archaebacterium
    • Heymann, J. A., W. A. Havelka and D. Oesterhelt (1993) Homologous overexpression of a light-driven anion pump in an archaebacterium. Mol. Microbiol. 7, 623-630.
    • (1993) Mol. Microbiol. , vol.7 , pp. 623-630
    • Heymann, J.A.1    Havelka, W.A.2    Oesterhelt, D.3
  • 5
    • 0027144770 scopus 로고
    • Projection structure of halorhodopsin from Halobacterium halobium at 6 Å resolution obtained by electron cryomicroscopy
    • Havelka, W. A., R. Henderson, J. A. Heymann and D. Oesterhelt (1993) Projection structure of halorhodopsin from Halobacterium halobium at 6 Å resolution obtained by electron cryomicroscopy. J. Mol. Biol. 234, 837-846.
    • (1993) J. Mol. Biol. , vol.234 , pp. 837-846
    • Havelka, W.A.1    Henderson, R.2    Heymann, J.A.3    Oesterhelt, D.4
  • 6
    • 0028959025 scopus 로고
    • Three-dimensional structure of halorhodopsin at 7 Å resolution
    • Havelka, W. A., R. Henderson and D. Oesterhelt (1995) Three-dimensional structure of halorhodopsin at 7 Å resolution. J. Mol. Biol. 247, 726-738.
    • (1995) J. Mol. Biol. , vol.247 , pp. 726-738
    • Havelka, W.A.1    Henderson, R.2    Oesterhelt, D.3
  • 7
    • 0024968418 scopus 로고
    • Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 1. Comparison of the photocycles of bacteriorhodopsin and halorhodopsin
    • Zimanyi, L., L. Keszthelyi and J. K. Lanyi (1989) Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 1. Comparison of the photocycles of bacteriorhodopsin and halorhodopsin. Biochemistry 28, 5165-5172.
    • (1989) Biochemistry , vol.28 , pp. 5165-5172
    • Zimanyi, L.1    Keszthelyi, L.2    Lanyi, J.K.3
  • 8
    • 0347736970 scopus 로고
    • A global fitting of halorhodopsin photocycle kinetics to complex kinetic schemes
    • Abstract
    • Dioumaev, A. K., J. Tittor and D. Oesterhelt (1993) A global fitting of halorhodopsin photocycle kinetics to complex kinetic schemes. 11th Int. Biophys. Cong. 1996. [Abstract]
    • (1993) 11th Int. Biophys. Cong. 1996
    • Dioumaev, A.K.1    Tittor, J.2    Oesterhelt, D.3
  • 9
    • 0347106467 scopus 로고
    • Kinetic intermediates of the halorhodopsin photocycle: Flash photolysis, global fitting and fitting to complex kinetic schemes
    • Abstract
    • Dioumaev, A. K. and D. Oesterhelt (1994) Kinetic intermediates of the halorhodopsin photocycle: flash photolysis, global fitting and fitting to complex kinetic schemes. 6th Int. Conf. on Retinal Proteins. [Abstract]
    • (1994) 6th Int. Conf. on Retinal Proteins
    • Dioumaev, A.K.1    Oesterhelt, D.2
  • 10
    • 0000948646 scopus 로고
    • The photocycle of the chloride pump halorhodopsin. II. Quantum yields and kinetic model
    • Oesterhelt, D., P. Hegemann and J. Tittor (1985) The photocycle of the chloride pump halorhodopsin. II. Quantum yields and kinetic model. EMBO J. 4, 2351-2356.
    • (1985) EMBO J. , vol.4 , pp. 2351-2356
    • Oesterhelt, D.1    Hegemann, P.2    Tittor, J.3
  • 11
    • 0025277893 scopus 로고
    • Activation parameters for the halorhodopsin photocycle: A phase lifetime spectroscopic study of the 520- and 640-nanometer intermediates
    • Spencer, D. B. and T. G. Dewey (1990) Activation parameters for the halorhodopsin photocycle: a phase lifetime spectroscopic study of the 520-and 640-nanometer intermediates. Biochemistry 29, 3140-3145.
    • (1990) Biochemistry , vol.29 , pp. 3140-3145
    • Spencer, D.B.1    Dewey, T.G.2
  • 12
    • 0001270797 scopus 로고
    • The photochemical cycle of halorhodopsin: Absolute spectra of intermediates obtained by flash photolysis and fast difference spectra measurements
    • Tittor, J., D. Oesterhelt, R. Maurer, H. Desel and R. Uhl (1987) The photochemical cycle of halorhodopsin: absolute spectra of intermediates obtained by flash photolysis and fast difference spectra measurements. Biophys. J. 52, 999-1006.
    • (1987) Biophys. J. , vol.52 , pp. 999-1006
    • Tittor, J.1    Oesterhelt, D.2    Maurer, R.3    Desel, H.4    Uhl, R.5
  • 13
    • 0024948732 scopus 로고
    • Halorhodopsin: A light-driven active chloride transport system
    • Zimanyi, L. and J. K. Lanyi (1989) Halorhodopsin: a light-driven active chloride transport system. Ann. N. Y. Acad. Sci. 574, 11-19.
    • (1989) Ann. N. Y. Acad. Sci. , vol.574 , pp. 11-19
    • Zimanyi, L.1    Lanyi, J.K.2
  • 14
    • 0024968421 scopus 로고
    • Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 2. Effects of anions on the halorhodopsin photocycle
    • Zimanyi, L. and J. K. Lanyi (1989) Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 2. Effects of anions on the halorhodopsin photocycle. Biochemistry 28, 5172-5178.
    • (1989) Biochemistry , vol.28 , pp. 5172-5178
    • Zimanyi, L.1    Lanyi, J.K.2
  • 16
    • 0028869129 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. the photochemical cycle
    • Váró, G., L. S. Brown, J. Sasaki, H. Kandori, A. Maeda, R. Needleman and J. K. Lanyi (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle. Biochemistry 34, 14490-14499.
    • (1995) Biochemistry , vol.34 , pp. 14490-14499
    • Váró, G.1    Brown, L.S.2    Sasaki, J.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 17
    • 0027050450 scopus 로고
    • Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism
    • Ames, J. B., J. Raap, J. Lugtenburg and R. A. Mathies (1992) Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism. Biochemistry 31, 12546-12554.
    • (1992) Biochemistry , vol.31 , pp. 12546-12554
    • Ames, J.B.1    Raap, J.2    Lugtenburg, J.3    Mathies, R.A.4
  • 18
    • 0023228638 scopus 로고
    • Resonance Raman studies of intermediates of the halorhodopsin photocycle
    • Diller, R., M. Stockburger, D. Oesterhelt and J. Tittor (1987) Resonance Raman studies of intermediates of the halorhodopsin photocycle. FEBS Lett. 217, 297-304.
    • (1987) FEBS Lett. , vol.217 , pp. 297-304
    • Diller, R.1    Stockburger, M.2    Oesterhelt, D.3    Tittor, J.4
  • 19
    • 0023661063 scopus 로고
    • Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance Raman spectroscopy
    • Fodor, S. P., R. A. Bogomolni and R. A. Mathies (1987) Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance Raman spectroscopy. Biochemistry 26, 6775-6778.
    • (1987) Biochemistry , vol.26 , pp. 6775-6778
    • Fodor, S.P.1    Bogomolni, R.A.2    Mathies, R.A.3
  • 20
    • 0024975543 scopus 로고
    • Low-temperature photoreactions of halorhodopsin. 2. Description of the photocycle and its intermediates
    • Zimanyi, L. and J. K. Lanyi (1989) Low-temperature photoreactions of halorhodopsin. 2. Description of the photocycle and its intermediates. Biochemistry 28, 1662-1666.
    • (1989) Biochemistry , vol.28 , pp. 1662-1666
    • Zimanyi, L.1    Lanyi, J.K.2
  • 22
    • 0028223284 scopus 로고
    • Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin
    • Braiman, M. S., T. J. Walter and D. M. Briercheck (1994) Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin. Biochemistry 33, 1629-1635.
    • (1994) Biochemistry , vol.33 , pp. 1629-1635
    • Braiman, M.S.1    Walter, T.J.2    Briercheck, D.M.3
  • 23
    • 0029040316 scopus 로고
    • Chemical reconstitution of a chloride pump inactivated by a single point mutation
    • Rüdiger, M., U. Haupts, K. Gerwert and D. Oesterhelt (1995) Chemical reconstitution of a chloride pump inactivated by a single point mutation. EMBO J. 14, 1599-1606.
    • (1995) EMBO J. , vol.14 , pp. 1599-1606
    • Rüdiger, M.1    Haupts, U.2    Gerwert, K.3    Oesterhelt, D.4
  • 24
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium
    • Lozier, R. H., R. A. Bogomolni and W. Stoeckenius (1975) Bacteriorhodopsin: a light-driven proton pump in Halobacterium halobium. Biophys. J. 15, 955-962.
    • (1975) Biophys. J. , vol.15 , pp. 955-962
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 25
    • 0021982340 scopus 로고
    • Picosecond events in the photochemical cycle of the light-driven chloride pump halorhodopsin
    • Polland, H. J., M. A. Franz, W. Zinth, W. Kaiser, P. Hegemann and D. Oesterhelt (1985) Picosecond events in the photochemical cycle of the light-driven chloride pump halorhodopsin. Biophys. J. 47, 55-59.
    • (1985) Biophys. J. , vol.47 , pp. 55-59
    • Polland, H.J.1    Franz, M.A.2    Zinth, W.3    Kaiser, W.4    Hegemann, P.5    Oesterhelt, D.6
  • 26
    • 0030728340 scopus 로고    scopus 로고
    • Evaluation of intrinsic chemical kinetics and transient product spectra from time-resolved spectroscopic data
    • Dioumaev, A. K. (1997) Evaluation of intrinsic chemical kinetics and transient product spectra from time-resolved spectroscopic data. Biophys. Chem. 67, 1-26.
    • (1997) Biophys. Chem. , vol.67 , pp. 1-26
    • Dioumaev, A.K.1
  • 28
    • 0021886417 scopus 로고
    • Resonance Raman study of binding of chloride to the chromophore of halorhodopsin
    • Maeda, A., T. Ogurusu, T. Yoshizawa and T. Kitagawa (1985) Resonance Raman study of binding of chloride to the chromophore of halorhodopsin. Biochemistry 24, 2517-2521.
    • (1985) Biochemistry , vol.24 , pp. 2517-2521
    • Maeda, A.1    Ogurusu, T.2    Yoshizawa, T.3    Kitagawa, T.4
  • 29
    • 0024515846 scopus 로고
    • Effects of various anions on the Raman spectrum of halorhodopsin
    • Pande, C., J. K. Lanyi and R. H. Callender (1989) Effects of various anions on the Raman spectrum of halorhodopsin. Biophys. J. 55, 425-431.
    • (1989) Biophys. J. , vol.55 , pp. 425-431
    • Pande, C.1    Lanyi, J.K.2    Callender, R.H.3
  • 30
    • 0028285064 scopus 로고
    • Anion-protein interactions during halorhodopsin pumping: Halide binding at the protonated Schiff base
    • Walter, T. J. and M. S. Braiman (1994) Anion-protein interactions during halorhodopsin pumping: halide binding at the protonated Schiff base. Biochemistry 33, 1724-1733.
    • (1994) Biochemistry , vol.33 , pp. 1724-1733
    • Walter, T.J.1    Braiman, M.S.2
  • 31
    • 0000005909 scopus 로고
    • Time resolved step scan FTIR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twists by assigning hydrogen out of plane (HOOP) bending vibrations
    • Weidlich, O. and F. Siebert (1993) Time resolved step scan FTIR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: identification of chromophore twists by assigning hydrogen out of plane (HOOP) bending vibrations. Appl. Spectrosc. 47, 1394-1400.
    • (1993) Appl. Spectrosc. , vol.47 , pp. 1394-1400
    • Weidlich, O.1    Siebert, F.2
  • 32
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • 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.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 33
    • 0023392472 scopus 로고
    • Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct
    • Braiman, M. S., P. L. Ahl and K. J. Rothschild (1987) Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct. Proc. Natl. Acad. Sci. USA 84, 5221-5225.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5221-5225
    • Braiman, M.S.1    Ahl, P.L.2    Rothschild, K.J.3
  • 34
    • 0031075390 scopus 로고    scopus 로고
    • Two bathointermediates in the bacteriorhodopsin photocycle distinguished by nanosecond time-resolved FTIR spectroscopy
    • Dioumaev, A. K. and M. S. Braiman (1997) Two bathointermediates in the bacteriorhodopsin photocycle distinguished by nanosecond time-resolved FTIR spectroscopy. J. Phys. Chem. 101, 1655-1662.
    • (1997) J. Phys. Chem. , vol.101 , pp. 1655-1662
    • Dioumaev, A.K.1    Braiman, M.S.2
  • 35
    • 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. Biophvs. J. 58, 597-608.
    • (1990) Biophvs. J. , vol.58 , pp. 597-608
    • Govindjee, R.1    Balashov, S.P.2    Ebrey, T.G.3
  • 36
    • 0008723652 scopus 로고
    • Two quantum absorption of ultrashort laser pulses by the bacteriorhodopsin chromophore
    • Edited by J. L. Rigaud, John Libbey Eurotext, Paris
    • Chizhov, I. V., M. Engelhard, A. V. Sharkov and B. Hess (1992) Two quantum absorption of ultrashort laser pulses by the bacteriorhodopsin chromophore. In Structure and Function of Retinal Proteins (Edited by J. L. Rigaud), pp. 171-173. John Libbey Eurotext, Paris.
    • (1992) Structure and Function of Retinal Proteins , pp. 171-173
    • Chizhov, I.V.1    Engelhard, M.2    Sharkov, A.V.3    Hess, B.4
  • 37
    • 84989737760 scopus 로고
    • Time resolved ultraviolet absorption changes in the photocycle of bacteriorhodopsin
    • Sharonov, A. Y., N. V. Tkachenko, V. V. Savransky and A. K. Dioumaev (1991) Time resolved ultraviolet absorption changes in the photocycle of bacteriorhodopsin. Photochem. Photobiol. 54, 889-895.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 889-895
    • Sharonov, A.Y.1    Tkachenko, N.V.2    Savransky, V.V.3    Dioumaev, A.K.4
  • 38
    • 0029116483 scopus 로고
    • Differences between the photocycles of halorhodopsin and the acid purple form of bacteriorhodopsin analyzed with millisecond time-resolved FTIR spectroscopy
    • Mitrovich, Q. M., K. G. Victor and M. S. Braiman (1995) Differences between the photocycles of halorhodopsin and the acid purple form of bacteriorhodopsin analyzed with millisecond time-resolved FTIR spectroscopy. Biophys. Chem. 56, 121-127.
    • (1995) Biophys. Chem. , vol.56 , pp. 121-127
    • Mitrovich, Q.M.1    Victor, K.G.2    Braiman, M.S.3
  • 39
    • 0021527915 scopus 로고
    • Primary photochemistry of bacteriorhodopsin: Comparison of Fourier transform infrared difference spectra with resonance Raman spectra
    • Rothschild, K. J., H. Marrero, M. Braiman and R. Mathies (1984) Primary photochemistry of bacteriorhodopsin: comparison of Fourier transform infrared difference spectra with resonance Raman spectra. Photochem. Photobiol. 40, 675-679.
    • (1984) Photochem. Photobiol. , vol.40 , pp. 675-679
    • Rothschild, K.J.1    Marrero, H.2    Braiman, M.3    Mathies, R.4
  • 40
    • 0026643216 scopus 로고
    • FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
    • Review
    • Rothschild, K. J. (1992) FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model. J. Bioenerg. Biomembr. 24, 147-167. [Review]
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 147-167
    • Rothschild, K.J.1
  • 41
    • 0021848415 scopus 로고
    • Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy
    • Smith, S. O., J. Lugtenburg and R. A. Mathies (1985) Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy. J. Membr. Biol. 85, 95-109.
    • (1985) J. Membr. Biol. , vol.85 , pp. 95-109
    • Smith, S.O.1    Lugtenburg, J.2    Mathies, R.A.3
  • 43
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • Smith, S. O., J. A. Pardoen, J. Lugtenburg and R. A. Mathies (1987) Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin. J. Chem. Phys. 91, 804-819.
    • (1987) J. Chem. Phys. , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 44
    • 0004713241 scopus 로고
    • Structure of the retinal chromophore in halorhodopsin. a resonance Raman study
    • Alshuth, T., M. Stockburger, P. Hegemann and D. Oesterhelt (1985) Structure of the retinal chromophore in halorhodopsin. A resonance Raman study. FEBS Lett. 179, 55-59.
    • (1985) FEBS Lett. , vol.179 , pp. 55-59
    • Alshuth, T.1    Stockburger, M.2    Hegemann, P.3    Oesterhelt, D.4
  • 45
    • 0028944068 scopus 로고
    • Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle
    • Sasaki, J., T. Yuzawa, H. Kandori, A. Maeda and H. Hamaguchi (1995) Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle. Biophys. J. 68, 2073-2080.
    • (1995) Biophys. J. , vol.68 , pp. 2073-2080
    • Sasaki, J.1    Yuzawa, T.2    Kandori, H.3    Maeda, A.4    Hamaguchi, H.5
  • 46
    • 33751156797 scopus 로고    scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: A nanosecond step-scan FTIR investigation of the KL to L transition
    • Hage, W., M. Kim, H. Frei and R. A. Mathies (1996) Protein dynamics in the bacteriorhodopsin photocycle: a nanosecond step-scan FTIR investigation of the KL to L transition. J. Phys. Chem. 100, 16026-16033.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16026-16033
    • Hage, W.1    Kim, M.2    Frei, H.3    Mathies, R.A.4
  • 47
    • 0028808334 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics
    • Váró, G., R. Needleman and J. K. Lanyi (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics. Biochemistry 34, 14500-14507.
    • (1995) Biochemistry , vol.34 , pp. 14500-14507
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 49
    • 84989726668 scopus 로고
    • Analysis of flash photolysis data by a global fit with multi-exponentials - II. Determination of consistent natural rate constants and the absorption spectra of the transient species in the bacteriorhodopsin photocycle from measurements at different temperatures
    • Maurer, R., J. Vogel and S. Schneider (1987) Analysis of flash photolysis data by a global fit with multi-exponentials - II. Determination of consistent natural rate constants and the absorption spectra of the transient species in the bacteriorhodopsin photocycle from measurements at different temperatures. Photochem. Photobiol. 46, 255-262.
    • (1987) Photochem. Photobiol. , vol.46 , pp. 255-262
    • Maurer, R.1    Vogel, J.2    Schneider, S.3
  • 50
    • 0020133090 scopus 로고
    • Procedure for testing kinetic models of the photocycle of bacteriorhodopsin
    • Nagle, J. F., L. A. Parodi and R. H. Lozier (1982) Procedure for testing kinetic models of the photocycle of bacteriorhodopsin. Biophys. J. 38, 161-174.
    • (1982) Biophys. J. , vol.38 , pp. 161-174
    • Nagle, J.F.1    Parodi, L.A.2    Lozier, R.H.3
  • 51
    • 0021514162 scopus 로고
    • Testing kinetic models for the bacteriorhodopsin photocycle. II. Inclusion of an O to M backreaction
    • Parodi, L. A., R. H. Lozier, S. M. Bhattacharjee and J. F. Nagle (1984) Testing kinetic models for the bacteriorhodopsin photocycle. II. Inclusion of an O to M backreaction. Photochem. Photobiol. 40, 501-506.
    • (1984) Photochem. Photobiol. , vol.40 , pp. 501-506
    • Parodi, L.A.1    Lozier, R.H.2    Bhattacharjee, S.M.3    Nagle, J.F.4
  • 52
    • 0023321923 scopus 로고
    • Flash spectroscopy of purple membrane
    • Xie, A. H., J. F. Nagle and R. H. Lozier (1987) Flash spectroscopy of purple membrane. Biophys. J. 51, 627-635.
    • (1987) Biophys. J. , vol.51 , pp. 627-635
    • Xie, A.H.1    Nagle, J.F.2    Lozier, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.