메뉴 건너뛰기




Volumn 74, Issue 3, 2001, Pages 495-503

Thermodynamics of the early steps in the photocycle of Natronobacterium pharaonis halorhodopsin. Influence of medium and of anion substitution

Author keywords

[No Author keywords available]

Indexed keywords

ANION; AZIDE; CHLORIDE; HALORHODOPSIN; PROTON PUMP;

EID: 0035470640     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2001)074<0495:TOTESI>2.0.CO;2     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0022484888 scopus 로고
    • Halorhodopsin - A light-driven chloride-ion pump
    • Lanyi, J. K. (1986) Halorhodopsin - a light-driven chloride-ion pump. Annu. Rev. Biophys. Biophys. Chem. 15, 11-28.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 11-28
    • Lanyi, J.K.1
  • 2
    • 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
  • 3
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Varo, G. (2000) Analogies between halorhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta 1460, 220-229.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Varo, G.1
  • 4
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt, D. (1998) The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8, 489-500.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 5
    • 0033587584 scopus 로고    scopus 로고
    • Existence of two L photointermediates of halorhodopsin from Halobacterium salinarum, differing in their protein and water FTIR bands
    • Chon, Y. S., H. Kandori, J. Sasaki, J. K. Lanyi, R. Needleman and A. Maeda (1999) Existence of two L photointermediates of halorhodopsin from Halobacterium salinarum, differing in their protein and water FTIR bands. Biochemistry 38, 9449-9455.
    • (1999) Biochemistry , vol.38 , pp. 9449-9455
    • Chon, Y.S.1    Kandori, H.2    Sasaki, J.3    Lanyi, J.K.4    Needleman, R.5    Maeda, A.6
  • 6
    • 0025157188 scopus 로고
    • The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins
    • Lanyi, J. K., A. Duschl and G. W. Hatfield (1990) The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins. J. Biol. Chem. 265, 1253-1260.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1253-1260
    • Lanyi, J.K.1    Duschl, A.2    Hatfield, G.W.3
  • 7
    • 0025064073 scopus 로고
    • Properties and photochemistry of a halorhodopsin from the haloalkalophile Natronobacterium pharaonis
    • Duschl, A., J. K. Lanyi and L. Zimanyi (1990) Properties and photochemistry of a halorhodopsin from the haloalkalophile Natronobacterium pharaonis. J. Biol. Chem. 265, 1261-1267.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1261-1267
    • Duschl, A.1    Lanyi, J.K.2    Zimanyi, L.3
  • 8
    • 0000948647 scopus 로고
    • The photocycle of the chloride pump halorhodopsin. 1. Azide catalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump
    • Hegemann, P., D. Oesterhelt and M. Steiner (1985) The photocycle of the chloride pump halorhodopsin. 1. Azide catalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump. EMBO J. 4, 2347-2350.
    • (1985) EMBO J. , vol.4 , pp. 2347-2350
    • Hegemann, P.1    Oesterhelt, D.2    Steiner, M.3
  • 9
    • 0033747017 scopus 로고    scopus 로고
    • Characterization of the proton-transporting photocycle of pharaonis halorhodopsin
    • Kulcsar, A., G. I. Groma, J. K. Lanyi and G. Varo (2000) Characterization of the proton-transporting photocycle of pharaonis halorhodopsin. Biophys. J. 79, 2705-2713.
    • (2000) Biophys. J. , vol.79 , pp. 2705-2713
    • Kulcsar, A.1    Groma, G.I.2    Lanyi, J.K.3    Varo, G.4
  • 10
    • 2342526764 scopus 로고
    • Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution
    • Braslavsky, S. E. and G. E. Heibel (1992) Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution. Chem. Rev. 92, 1381-1410.
    • (1992) Chem. Rev. , vol.92 , pp. 1381-1410
    • Braslavsky, S.E.1    Heibel, G.E.2
  • 11
    • 11744337523 scopus 로고    scopus 로고
    • 3(MLCT) state of ruthenium(II) bipyridine cyano complexes in the presence of salts. A case of the entropy-enthalpy compensation effect
    • 3(MLCT) state of ruthenium(II) bipyridine cyano complexes in the presence of salts. A case of the entropy-enthalpy compensation effect. J. Phys. Chem. B 102, 6231-6238.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6231-6238
    • Borsarelli, C.D.1    Braslavsky, S.E.2
  • 13
    • 0035961494 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation in a photocycle: The K to L transition in sensory rhodopsin II from Natronobacterium pharaonis
    • Losi, A., A. A. Wegener, M. Engelhardt and S. E. Braslavsky (2001) Enthalpy-entropy compensation in a photocycle: the K to L transition in sensory rhodopsin II from Natronobacterium pharaonis. J. Am. Chem. Soc. 123, 1766-1767.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1766-1767
    • Losi, A.1    Wegener, A.A.2    Engelhardt, M.3    Braslavsky, S.E.4
  • 14
    • 0028869129 scopus 로고
    • Light-driven chloride-ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle
    • Varo, 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 44, 14 490-14 499.
    • (1995) Biochemistry , vol.44 , pp. 14490-14499
    • Varo, G.1    Brown, L.S.2    Sasaki, J.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 15
    • 0030850650 scopus 로고    scopus 로고
    • Chromophore-anion interactios in halorhodopsin from Natronobacterium pharaonis probed by time-resolved resonance Raman spectroscopy
    • Gerscher, S., M. Mylrajan, P. Hildebrandt, M. H. Baron, R. Müller and M. Engelhard (1997) Chromophore-anion interactios in halorhodopsin from Natronobacterium pharaonis probed by time-resolved resonance Raman spectroscopy. Biochemistry 36, 11 012-11 020.
    • (1997) Biochemistry , vol.36 , pp. 11012-11020
    • Gerscher, S.1    Mylrajan, M.2    Hildebrandt, P.3    Baron, M.H.4    Müller, R.5    Engelhard, M.6
  • 16
    • 0032963356 scopus 로고    scopus 로고
    • Purification of histidine tagged bacteriorhodopsin, pharaonis halorhodopsin and pharaonis sensory rhodopsin II functionally expressed in Escherichia coli
    • Hohenfeld, I. P., A. A. Wegener and M. Engelhard (1999) Purification of histidine tagged bacteriorhodopsin, pharaonis halorhodopsin and pharaonis sensory rhodopsin II functionally expressed in Escherichia coli. FEBS Lett. 442, 198-202.
    • (1999) FEBS Lett. , vol.442 , pp. 198-202
    • Hohenfeld, I.P.1    Wegener, A.A.2    Engelhard, M.3
  • 17
    • 0032804617 scopus 로고    scopus 로고
    • Time-resolved absorption and photothermal measurements with recombinant sensory rhodopsin II from Natronobacterium pharaonis
    • Losi, A., A. A. Wegener, M. Engelhard, W. Gärtner and S. E. Braslavsky (1999) Time-resolved absorption and photothermal measurements with recombinant sensory rhodopsin II from Natronobacterium pharaonis. Biophys. J. 77, 3277-3286.
    • (1999) Biophys. J. , vol.77 , pp. 3277-3286
    • Losi, A.1    Wegener, A.A.2    Engelhard, M.3    Gärtner, W.4    Braslavsky, S.E.5
  • 18
    • 0028286154 scopus 로고
    • Blue halorhodopsin from Natronobacterium pharaonis - Wavelength regulation by anions
    • Scharf, B. and M. Engelhard (1994) Blue halorhodopsin from Natronobacterium pharaonis - wavelength regulation by anions. Biochemistry 33, 6387-6393.
    • (1994) Biochemistry , vol.33 , pp. 6387-6393
    • Scharf, B.1    Engelhard, M.2
  • 19
    • 0001386064 scopus 로고
    • Removal of methyl groups from retinal controls the activity of bacteriorhodopsin
    • Gärtner, W., P. Towner, H. Hopf and D. Oesterhelt (1983) Removal of methyl groups from retinal controls the activity of bacteriorhodopsin. Biochemistry 22, 2637-2644.
    • (1983) Biochemistry , vol.22 , pp. 2637-2644
    • Gärtner, W.1    Towner, P.2    Hopf, H.3    Oesterhelt, D.4
  • 20
    • 33845379032 scopus 로고
    • Simultaneous determination of photoreaction dynamics and energetics using pulsed, time-resolved photoacoustic calorimetry
    • Rudzki-Small, J. E., J. L. Goodman and K. S. Peters (1985) Simultaneous determination of photoreaction dynamics and energetics using pulsed, time-resolved photoacoustic calorimetry. J. Am. Chem. Soc. 107, 7849-7854.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7849-7854
    • Rudzki-Small, J.E.1    Goodman, J.L.2    Peters, K.S.3
  • 21
    • 0026599491 scopus 로고
    • Analysis of photoacoustic wave-forms using the nonlinear least-squares method
    • Rudzki-Small, J. R., L. J. Libertini and E. W. Small (1992) Analysis of photoacoustic wave-forms using the nonlinear least-squares method. Biophys. Chem. 42, 29-48.
    • (1992) Biophys. Chem. , vol.42 , pp. 29-48
    • Rudzki-Small, J.R.1    Libertini, L.J.2    Small, E.W.3
  • 22
    • 0031176623 scopus 로고    scopus 로고
    • Nature of the water structure inside the pools of reversed micelles sensed by laser-induced optoacoustic spectroscopy
    • Borsarelli, C. D. and S. E. Braslavsky (1997) Nature of the water structure inside the pools of reversed micelles sensed by laser-induced optoacoustic spectroscopy. J. Phys. Chem. B 101, 6036-6042.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 6036-6042
    • Borsarelli, C.D.1    Braslavsky, S.E.2
  • 23
    • 0028918464 scopus 로고
    • Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila
    • van Brederode, M. E., T. Gensch, W. D. Hoff, K. J. Hellingwerf and S. E. Braslavsky (1995) Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys. J. 68, 1101-1109.
    • (1995) Biophys. J. , vol.68 , pp. 1101-1109
    • Van Brederode, M.E.1    Gensch, T.2    Hoff, W.D.3    Hellingwerf, K.J.4    Braslavsky, S.E.5
  • 24
    • 0028301764 scopus 로고
    • Photochemical energy storage and volume changes in the microsecond time range in bacterial photosynthesis. A laser induced optoacoustic study
    • Malkin, S., M. S. Churio, S. Shochat and S. E. Braslavsky (1994) Photochemical energy storage and volume changes in the microsecond time range in bacterial photosynthesis. A laser induced optoacoustic study. J. Photochem. Photobiol. B: Biol. 23, 79-85.
    • (1994) J. Photochem. Photobiol. B: Biol. , vol.23 , pp. 79-85
    • Malkin, S.1    Churio, M.S.2    Shochat, S.3    Braslavsky, S.E.4
  • 25
    • 0031021093 scopus 로고    scopus 로고
    • Recombinant type A and B phytochromes from potato. Transient absorption spectroscopy
    • Ruddat, A., P. Schmidt, C. Gatz, S. E. Braslavsky, W. Gärtner and K. Schaffner (1997) Recombinant type A and B phytochromes from potato. Transient absorption spectroscopy. Biochemistry 36, 103-111.
    • (1997) Biochemistry , vol.36 , pp. 103-111
    • Ruddat, A.1    Schmidt, P.2    Gatz, C.3    Braslavsky, S.E.4    Gärtner, W.5    Schaffner, K.6
  • 26
    • 0033579148 scopus 로고    scopus 로고
    • Structural volume changes upon photoexcitation of porphyrins: Role of the nitrogen-water interactions
    • Gensch, T., C. Viappiani and S. E. Braslavsky (1999) Structural volume changes upon photoexcitation of porphyrins: role of the nitrogen-water interactions. J. Am. Chem. Soc. 121, 10 573-10 582.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10573-10582
    • Gensch, T.1    Viappiani, C.2    Braslavsky, S.E.3
  • 27
    • 0034075676 scopus 로고    scopus 로고
    • Charge motions during the photocycle of pharaonis halorhodopsin
    • Ludmann, K., G. Ibron, J. K. Lanyi and G. Varo (2000) Charge motions during the photocycle of pharaonis halorhodopsin. Biophys. J. 78, 959-966.
    • (2000) Biophys. J. , vol.78 , pp. 959-966
    • Ludmann, K.1    Ibron, G.2    Lanyi, J.K.3    Varo, G.4
  • 28
    • 0029948137 scopus 로고    scopus 로고
    • Volume and enthalpy changes in the early steps of bacteriorhodopsin photocycle studied by time-resolved photoacoustics
    • Zhang, D. and D. Mauzerall (1996) Volume and enthalpy changes in the early steps of bacteriorhodopsin photocycle studied by time-resolved photoacoustics. Biophys. J. 71, 381-388.
    • (1996) Biophys. J. , vol.71 , pp. 381-388
    • Zhang, D.1    Mauzerall, D.2
  • 29
    • 22444453365 scopus 로고    scopus 로고
    • Volume and enthalpy changes upon photoexcitation of bovine rhodopsin derived from optoacoustic studies by using an equilibrium between bathorhodopsin and blue-shifted intermediate
    • Gensch, T., J. Strassburger, W. Gärtner and S. E. Braslavsky (1998) Volume and enthalpy changes upon photoexcitation of bovine rhodopsin derived from optoacoustic studies by using an equilibrium between bathorhodopsin and blue-shifted intermediate. Isr. J. Chem. 38, 231-236.
    • (1998) Isr. J. Chem. , vol.38 , pp. 231-236
    • Gensch, T.1    Strassburger, J.2    Gärtner, W.3    Braslavsky, S.E.4
  • 30
    • 0032992050 scopus 로고    scopus 로고
    • Time-resolved absorption and photothermal measurements with sensory rhodopsin I from Halobacterium salinarum
    • Losi, A., S. E. Braslavsky, W. Gärtner and J. L. Spudich (1999) Time-resolved absorption and photothermal measurements with sensory rhodopsin I from Halobacterium salinarum. Biophys. J. 76, 2183-2191.
    • (1999) Biophys. J. , vol.76 , pp. 2183-2191
    • Losi, A.1    Braslavsky, S.E.2    Gärtner, W.3    Spudich, J.L.4
  • 31
    • 0034023143 scopus 로고    scopus 로고
    • Aspartate 75 mutation in sensory rhodopsin II from Natronobacterium pharaonis does not influence the production of the K-like intermediate, but strongly affects its relaxation pathway
    • Losi, A., A. A. Wegener, M. Engelhard, W. Gärtner and S. E. Braslavsky (2000) Aspartate 75 mutation in sensory rhodopsin II from Natronobacterium pharaonis does not influence the production of the K-like intermediate, but strongly affects its relaxation pathway. Biophys. J. 78, 2581-2589.
    • (2000) Biophys. J. , vol.78 , pp. 2581-2589
    • Losi, A.1    Wegener, A.A.2    Engelhard, M.3    Gärtner, W.4    Braslavsky, S.E.5
  • 32
    • 0028454391 scopus 로고
    • The interaction of melanin with 8-methoxypsoralen: Quenching effect on radiative and nonradiative transitions. A fluorescence and pulsed photoacoustic study
    • Losi, A., C. Viappiani and P. R. Crippa (1994) The interaction of melanin with 8-methoxypsoralen: quenching effect on radiative and nonradiative transitions. A fluorescence and pulsed photoacoustic study. Photochem. Photobiol. 59, 596-602.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 596-602
    • Losi, A.1    Viappiani, C.2    Crippa, P.R.3
  • 33
    • 0033825077 scopus 로고    scopus 로고
    • Temperature dependent volume change of initial step of the photoreaction of photoactive yellow protein (PYP) studied by the transient grating
    • Takeshita, K., N. Hirota, Y. Imamoto, M. Kataoka, F. Tokunaga and M. Terazima (2000) Temperature dependent volume change of initial step of the photoreaction of photoactive yellow protein (PYP) studied by the transient grating. J. Am. Chem. Soc. 122, 8524-8528.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8524-8528
    • Takeshita, K.1    Hirota, N.2    Imamoto, Y.3    Kataoka, M.4    Tokunaga, F.5    Terazima, M.6
  • 34
    • 0030597107 scopus 로고    scopus 로고
    • Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis
    • Engelhard, M., B. Scharf and F. Siebert (1996) Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis. FEBS Lett. 95, 195-198.
    • (1996) FEBS Lett. , vol.95 , pp. 195-198
    • Engelhard, M.1    Scharf, B.2    Siebert, F.3
  • 36
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution
    • Kolbe, M., H. Besir, L. O. Essen and D. Oesterhelt (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution. Science 288, 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 38
    • 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. Briecheck (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    Briecheck, D.M.3
  • 39
    • 0001199087 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Conformational fluctuation and induced-fit
    • Qian, H. (1998) Entropy-enthalpy compensation: conformational fluctuation and induced-fit. J. Chem. Phys. 109, 10 015-10 017.
    • (1998) J. Chem. Phys. , vol.109 , pp. 10015-10017
    • Qian, H.1
  • 40
    • 33645831413 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Perturbation and relaxation in thermodynamic systems
    • Qian, H. and J. J. Hopfield (1996) Entropy-enthalpy compensation: perturbation and relaxation in thermodynamic systems. J. Chem. Phys. 105, 9292-9298.
    • (1996) J. Chem. Phys. , vol.105 , pp. 9292-9298
    • Qian, H.1    Hopfield, J.J.2
  • 41
    • 0034335274 scopus 로고    scopus 로고
    • Time-resolved thermodynamic changes photoinduced in 5.12-trans-locked bacteriorhodopsin. Evidence that retinal isomerization is required for protein activation
    • Losi, A., I. Michler, W. Gärtner and S. E. Braslavsky (2000) Time-resolved thermodynamic changes photoinduced in 5.12-trans-locked bacteriorhodopsin. Evidence that retinal isomerization is required for protein activation. Photochem. Photobiol. 72, 590-597.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 590-597
    • Losi, A.1    Michler, I.2    Gärtner, W.3    Braslavsky, S.E.4
  • 42
    • 0028808334 scopus 로고
    • Light driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics
    • Varo, 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, 14 500-14 507.
    • (1995) Biochemistry , vol.34 , pp. 14500-14507
    • Varo, G.1    Needleman, R.2    Lanyi, J.K.3
  • 43
    • 0029117029 scopus 로고
    • Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle
    • Varo, G. and J. K. Lanyi (1995) Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle. Biochemistry 34, 12 162-12 169.
    • (1995) Biochemistry , vol.34 , pp. 12162-12169
    • Varo, G.1    Lanyi, J.K.2
  • 44
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Varo, G. and J. K. Lanyi (1991) Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30, 5016-5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Varo, G.1    Lanyi, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.