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Volumn 90, Issue 11, 2006, Pages 4224-4235

Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PHOTOACTIVE YELLOW PROTEIN;

EID: 33744912217     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.074765     Document Type: Article
Times cited : (48)

References (52)
  • 1
    • 2942752112 scopus 로고    scopus 로고
    • Initial events in the photocycle of photoactive yellow protein
    • Kort, R., K. J. Hellingwerf, and R. B. G. Ravelli. 2004. Initial events in the photocycle of photoactive yellow protein. J. Biol. Chem. 279:26417-26424.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26417-26424
    • Kort, R.1    Hellingwerf, K.J.2    Ravelli, R.B.G.3
  • 2
    • 4644242592 scopus 로고    scopus 로고
    • Structural heterogeneity of cryotrapped intermediates in the bacterial blue light photoreceptor, photoactive yellow protein
    • Anderson, S., V. Srajer, and K. Moffat. 2004. Structural heterogeneity of cryotrapped intermediates in the bacterial blue light photoreceptor, photoactive yellow protein. Photochem. Photobiol. 80:7-14.
    • (2004) Photochem. Photobiol. , vol.80 , pp. 7-14
    • Anderson, S.1    Srajer, V.2    Moffat, K.3
  • 3
    • 0031904189 scopus 로고    scopus 로고
    • Ultrafast time-resolved crystallography
    • Moffat, K. 1998. Ultrafast time-resolved crystallography. Nat. Struct. Biol. 5(Suppl):641-643.
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.SUPPL. , pp. 641-643
    • Moffat, K.1
  • 6
    • 0035354587 scopus 로고    scopus 로고
    • Time-resolved biochemical crystallography: A mechanistic perspective
    • Moffat, K. 2001. Time-resolved biochemical crystallography: a mechanistic perspective. Chem. Rev. 101:1569-1581.
    • (2001) Chem. Rev. , vol.101 , pp. 1569-1581
    • Moffat, K.1
  • 7
    • 0037452676 scopus 로고    scopus 로고
    • Crystal structure of a photoactive yellow protein from a sensor histidine kinase: Conformational variability and signal transduction
    • Rajagopal, S., and K. Moffat. 2003. Crystal structure of a photoactive yellow protein from a sensor histidine kinase: conformational variability and signal transduction. Proc. Natl. Acad. Sci. USA. 100:1649-1654.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1649-1654
    • Rajagopal, S.1    Moffat, K.2
  • 9
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 A° resolution of an early protein photocycle intermediate
    • Genick, U. K., S. M. Soltis, P. Kuhn, I. L. Canestrelli, and E. D. Getzoff. 1998. Structure at 0.85 A° resolution of an early protein photocycle intermediate. Nature. 392:206-209.
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 10
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8 A° resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds
    • Ren, Z., B. Perman, V. Srajer, T. Y. Teng, C. Pradervand, D. Bourgeois, F. Schotte, T. Ursby, R. Kort, M. Wulff, and K. Moffat. 2001. A molecular movie at 1.8 A° resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds. Biochemistry. 40:13788-13801.
    • (2001) Biochemistry , vol.40 , pp. 13788-13801
    • Ren, Z.1    Perman, B.2    Srajer, V.3    Teng, T.Y.4    Pradervand, C.5    Bourgeois, D.6    Schotte, F.7    Ursby, T.8    Kort, R.9    Wulff, M.10    Moffat, K.11
  • 11
    • 0037342350 scopus 로고    scopus 로고
    • Application of singular value decomposition to the analysis of time-resolved macromolecular x-ray data
    • Schmidt, M., S. Rajagopal, Z. Ren, and K. Moffat. 2003. Application of singular value decomposition to the analysis of time-resolved macromolecular x-ray data. Biophys. J. 84:2112-2129.
    • (2003) Biophys. J. , vol.84 , pp. 2112-2129
    • Schmidt, M.1    Rajagopal, S.2    Ren, Z.3    Moffat, K.4
  • 13
    • 4344653824 scopus 로고    scopus 로고
    • Analytical trapping: Extraction of time-independent structures from time-dependent crystallographic data
    • Rajagopal, S., K. S. Kostov, and K. Moffat. 2004. Analytical trapping: extraction of time-independent structures from time-dependent crystallographic data. J. Struct. Biol. 147:211-222.
    • (2004) J. Struct. Biol. , vol.147 , pp. 211-222
    • Rajagopal, S.1    Kostov, K.S.2    Moffat, K.3
  • 16
    • 11844294715 scopus 로고    scopus 로고
    • A structural pathway for signaling in the E46Q mutant of photoactive yellow protein
    • Rajagopal, S., S. Anderson, V. Srajer, M. Schmidt, R. Pahl, and K. Moffat. 2005. A structural pathway for signaling in the E46Q mutant of photoactive yellow protein. Structure. 13:55-63.
    • (2005) Structure , vol.13 , pp. 55-63
    • Rajagopal, S.1    Anderson, S.2    Srajer, V.3    Schmidt, M.4    Pahl, R.5    Moffat, K.6
  • 17
    • 21244491885 scopus 로고    scopus 로고
    • Using time-resolved vibrational spectroscopy for interrogation of structural dynamics
    • Nibbering, E. T. J., H. Fidder, and E. Pines. 2005. Using time-resolved vibrational spectroscopy for interrogation of structural dynamics. Annu. Rev. Phys. Chem. 56:337-367.
    • (2005) Annu. Rev. Phys. Chem. , vol.56 , pp. 337-367
    • Nibbering, E.T.J.1    Fidder, H.2    Pines, E.3
  • 18
    • 0026788194 scopus 로고
    • Forces, bond lengths, and reactivity: Fundamental insight into the mechanism of enzyme catalysis
    • Tonge, P. J., and P. R. Carey. 1992. Forces, bond lengths, and reactivity: fundamental insight into the mechanism of enzyme catalysis. Biochemistry. 31:9122-9125.
    • (1992) Biochemistry , vol.31 , pp. 9122-9125
    • Tonge, P.J.1    Carey, P.R.2
  • 19
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • Xie, A., L. Kelemen, J. Hendriks, B. J. White, K. J. Hellingwerf, and W. D. Hoff. 2001. Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation. Biochemistry. 40:1510-1517.
    • (2001) Biochemistry , vol.40 , pp. 1510-1517
    • Xie, A.1    Kelemen, L.2    Hendriks, J.3    White, B.J.4    Hellingwerf, K.J.5    Hoff, W.D.6
  • 20
    • 0038558401 scopus 로고    scopus 로고
    • Comparison of the photochemical reaction of photoactive yellow protein in crystal with reaction in solution
    • Mano, E., H. Kamikubo, Y. Imamoto, and M. Kataoka. 2003. Comparison of the photochemical reaction of photoactive yellow protein in crystal with reaction in solution. Spectrosc.-Int. J. 17:345-353.
    • (2003) Spectrosc.-Int. J. , vol.17 , pp. 345-353
    • Mano, E.1    Kamikubo, H.2    Imamoto, Y.3    Kataoka, M.4
  • 22
    • 0027728765 scopus 로고
    • A fast and portable microspectrophotometer for protein crystallography
    • Hadfield, A., and J. Hajdu. 1993. A fast and portable microspectrophotometer for protein crystallography. J. Appl. Crystallogr. 26:839-842.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 839-842
    • Hadfield, A.1    Hajdu, J.2
  • 23
    • 0032857645 scopus 로고    scopus 로고
    • Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophila
    • Hendriks, J., I. H. M. van Stokkum, W. Crielaard, and K. J. Hellingwerf. 1999. Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophila. FEBS Lett. 458:252-256.
    • (1999) FEBS Lett. , vol.458 , pp. 252-256
    • Hendriks, J.1    Van Stokkum, I.H.M.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 25
    • 0037305871 scopus 로고    scopus 로고
    • Deuterium isotope effects in the photocycle transitions of the photoactive yellow protein
    • Hendriks, J., I. H. M. van Stokkum, and K. J. Hellingwerf. 2003. Deuterium isotope effects in the photocycle transitions of the photoactive yellow protein. Biophys. J. 84:1180-1191.
    • (2003) Biophys. J. , vol.84 , pp. 1180-1191
    • Hendriks, J.1    Van Stokkum, I.H.M.2    Hellingwerf, K.J.3
  • 26
    • 0028898295 scopus 로고
    • Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals
    • Ng, K., E. D. Getzoff, and K. Moffat. 1995. Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals. Biochemistry. 34:879-890.
    • (1995) Biochemistry , vol.34 , pp. 879-890
    • Ng, K.1    Getzoff, E.D.2    Moffat, K.3
  • 33
    • 0024730905 scopus 로고
    • Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery
    • Meyer, T. E., G. Tollin, J. H. Hazzard, and M. A. Cusanovich. 1989. Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery. Biophys. J. 56:559-564.
    • (1989) Biophys. J. , vol.56 , pp. 559-564
    • Meyer, T.E.1    Tollin, G.2    Hazzard, J.H.3    Cusanovich, M.A.4
  • 34
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
    • Meyer, T. E., E. Yakali, M. A. Cusanovich, and G. Tollin. 1987. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 26:418-423.
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 35
    • 0041846661 scopus 로고    scopus 로고
    • pH dependence of the photocycle kinetics of the E46Q mutant of photoactive yellow protein: Protonation equilibrium between I1 and I2 intermediates, chromophore deprotonation by hydroxyl uptake, and protonation relaxation of the dark state
    • Borucki, B., H. Otto, C. P. Joshi, C. Gasperi, M. A. Cusanovich, S. Devanathan, G. Tollin, and M. P. Heyn. 2003. pH dependence of the photocycle kinetics of the E46Q mutant of photoactive yellow protein: protonation equilibrium between I1 and I2 intermediates, chromophore deprotonation by hydroxyl uptake, and protonation relaxation of the dark state. Biochemistry. 42:8780-8790.
    • (2003) Biochemistry , vol.42 , pp. 8780-8790
    • Borucki, B.1    Otto, H.2    Joshi, C.P.3    Gasperi, C.4    Cusanovich, M.A.5    Devanathan, S.6    Tollin, G.7    Heyn, M.P.8
  • 36
    • 0344990168 scopus 로고    scopus 로고
    • Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion
    • Chen, E., T. Gensch, A. B. Gross, J. Hendriks, K. J. Hellingwerf, and D. S. Kliger. 2003. Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion. Biochemistry. 42:2062-2071.
    • (2003) Biochemistry , vol.42 , pp. 2062-2071
    • Chen, E.1    Gensch, T.2    Gross, A.B.3    Hendriks, J.4    Hellingwerf, K.J.5    Kliger, D.S.6
  • 37
    • 19944390971 scopus 로고    scopus 로고
    • Hydrogen-bond network probed by time-resolved optoacoustic spectroscopy: Photoactive yellow protein and the effect of E46Q and E46A mutations
    • Losi, A., T. Gensch, M. A. v. d. Horst, K. J. Hellingwerf, and S. E. Braslavsky. 2005. Hydrogen-bond network probed by time-resolved optoacoustic spectroscopy: photoactive yellow protein and the effect of E46Q and E46A mutations. Phys. Chem. Chem. Phys. 10:2229-2236.
    • (2005) Phys. Chem. Chem. Phys. , vol.10 , pp. 2229-2236
    • Losi, A.1    Gensch, T.2    Horst, M.A.V.D.3    Hellingwerf, K.J.4    Braslavsky, S.E.5
  • 38
    • 0035859406 scopus 로고    scopus 로고
    • Photocycle dynamics and vibrational spectroscopy of the E46Q mutant of photoactive yellow protein
    • Zhou, Y., L. Ujj, T. E. Meyer, M. A. Cusanovich, and G. H. Atkinson. 2001. Photocycle dynamics and vibrational spectroscopy of the E46Q mutant of photoactive yellow protein. J. Phys. Chem. A. 105:5719-5726.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 5719-5726
    • Zhou, Y.1    Ujj, L.2    Meyer, T.E.3    Cusanovich, M.A.4    Atkinson, G.H.5
  • 39
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • Ellis, R. J., and A. P. Minton. 2003. Cell biology: join the crowd. Nature. 425:27-28.
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 40
    • 0037137227 scopus 로고    scopus 로고
    • Light-induced global conformational change of photoactive yellow protein in solution
    • Imamoto, Y., H. Kamikubo, M. Harigai, N. Shimizu, and M. Kataoka. 2002. Light-induced global conformational change of photoactive yellow protein in solution. Biochemistry. 41:13595-13601.
    • (2002) Biochemistry , vol.41 , pp. 13595-13601
    • Imamoto, Y.1    Kamikubo, H.2    Harigai, M.3    Shimizu, N.4    Kataoka, M.5
  • 41
  • 42
    • 0034745934 scopus 로고    scopus 로고
    • Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy
    • Brudler, R., R. Rammelsberg, T. T. Woo, E. D. Getzoff, and K. Gerwert. 2001. Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy. Nat. Struct. Biol. 8:265-270.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 265-270
    • Brudler, R.1    Rammelsberg, R.2    Woo, T.T.3    Getzoff, E.D.4    Gerwert, K.5
  • 45
    • 2942533032 scopus 로고    scopus 로고
    • Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein
    • Anderson, S., V. Srajer, R. Pahl, S. Rajagopal, F. Schotte, P. Anfinrud, M. Wulff, and K. Moffat. 2004. Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein. Structure. 12:1039-1045.
    • (2004) Structure , vol.12 , pp. 1039-1045
    • Anderson, S.1    Srajer, V.2    Pahl, R.3    Rajagopal, S.4    Schotte, F.5    Anfinrud, P.6    Wulff, M.7    Moffat, K.8
  • 46
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton, A. B. 1982. How crowded is the cytoplasm? Cell. 30:345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 47
    • 21744447700 scopus 로고    scopus 로고
    • Controlled reduction of the humidity induces a shortcut recovery reaction in the photocycle of photoactive yellow protein
    • van der Horst, M. A., I. H. M. van Stokkum, N. A. Dencher, and K. J. Hellingwerf. 2005. Controlled reduction of the humidity induces a shortcut recovery reaction in the photocycle of photoactive yellow protein. Biochemistry. 44:9160-9167.
    • (2005) Biochemistry , vol.44 , pp. 9160-9167
    • Van Der Horst, M.A.1    Van Stokkum, I.H.M.2    Dencher, N.A.3    Hellingwerf, K.J.4
  • 48
    • 17844374336 scopus 로고    scopus 로고
    • Predicting the signaling state of photoactive yellow protein
    • Vreede, J., W. Crielaard, K. J. Hellingwerf, and P. G. Bolhuis. 2005. Predicting the signaling state of photoactive yellow protein. Biophys. J. 88:3525-3535.
    • (2005) Biophys. J. , vol.88 , pp. 3525-3535
    • Vreede, J.1    Crielaard, W.2    Hellingwerf, K.J.3    Bolhuis, P.G.4
  • 50
    • 2942599831 scopus 로고    scopus 로고
    • Short hydrogen bonds in photoactive yellow protein
    • Anderson, S., S. Crosson, and K. Moffat. 2004. Short hydrogen bonds in photoactive yellow protein. Acta Crystallogr. D. 60:1008-1016.
    • (2004) Acta Crystallogr. D. , vol.60 , pp. 1008-1016
    • Anderson, S.1    Crosson, S.2    Moffat, K.3
  • 51
    • 0346850583 scopus 로고    scopus 로고
    • Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate
    • Derix, N. M., R. W. Wechselberger, M. A. Van Der Horst, K. J. Hellingwerf, R. Boelens, R. Kaptein, and N. A. Van Nuland. 2003. Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate. Biochemistry. 42:14501-14506.
    • (2003) Biochemistry , vol.42 , pp. 14501-14506
    • Derix, N.M.1    Wechselberger, R.W.2    Van Der Horst, M.A.3    Hellingwerf, K.J.4    Boelens, R.5    Kaptein, R.6    Van Nuland, N.A.7
  • 52
    • 11844255732 scopus 로고    scopus 로고
    • Resolving protein structure dynamically
    • Yeremenko, S., and K. J. Hellingwerf. 2005. Resolving protein structure dynamically. Structure. 13:4-6.
    • (2005) Structure , vol.13 , pp. 4-6
    • Yeremenko, S.1    Hellingwerf, K.J.2


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