메뉴 건너뛰기




Volumn 78, Issue 2, 2003, Pages 131-137

Characterization of Photocycle Intermediates in Crystalline Photoactive Yellow Protein

Author keywords

[No Author keywords available]

Indexed keywords

PHOTOACTIVE YELLOW PROTEIN;

EID: 0242302505     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2003)078<0131:COPIIC>2.0.CO;2     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 0034048749 scopus 로고    scopus 로고
    • Key issues in the photochemistry and signalling-state formation of photosensor proteins
    • Hellingwerf, K. J. (2000) Key issues in the photochemistry and signalling-state formation of photosensor proteins. J. Photochem. Photobiol. B: Biol. 54, 94-102.
    • (2000) J. Photochem. Photobiol. B: Biol. , vol.54 , pp. 94-102
    • Hellingwerf, K.J.1
  • 2
    • 0029803844 scopus 로고    scopus 로고
    • Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy
    • Imamoto, Y., M. Kataoka and F. Tokunaga (1996) Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy. Biochemistry 35, 14047-14053.
    • (1996) Biochemistry , vol.35 , pp. 14047-14053
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3
  • 3
    • 84989696264 scopus 로고
    • Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila
    • Hoff, W. D., S. L. S. Kwa, R. Van Grondelle and K. J. Hellingwerf (1992) Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila. Photochem. Photobiol. 56, 529-539.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 529-539
    • Hoff, W.D.1    Kwa, S.L.S.2    Van Grondelle, R.3    Hellingwerf, K.J.4
  • 4
    • 0031808072 scopus 로고    scopus 로고
    • New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy
    • Ujj, L., S. Devanathan, T. E. Meyer, M. A. Cusanovich, G. Tollin and G. H. Atkinson (1998) New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy. Biophys. J. 75, 406-412.
    • (1998) Biophys. J. , vol.75 , pp. 406-412
    • Ujj, L.1    Devanathan, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Tollin, G.5    Atkinson, G.H.6
  • 5
    • 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
  • 7
    • 0029964634 scopus 로고    scopus 로고
    • Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein
    • Kort, R., H. Vonk, X. Xu, W. D. Hoff, W. Crielaard and K. J. Hellingwerf (1996) Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein. FEBS Lett. 382, 73-78.
    • (1996) FEBS Lett. , vol.382 , pp. 73-78
    • Kort, R.1    Vonk, H.2    Xu, X.3    Hoff, W.D.4    Crielaard, W.5    Hellingwerf, K.J.6
  • 8
  • 9
    • 0037156178 scopus 로고    scopus 로고
    • The primary photoreaction of photoactive yellow protein (PYP): Anisotropy changes and excitation wavelength dependence
    • Gensch, T., C. C. Gradinam, I. H. M. van Stokkum, J. Hendriks, K. J. Hellingwerf and R. van Grondelle (2002) The primary photoreaction of photoactive yellow protein (PYP): anisotropy changes and excitation wavelength dependence. Chem. Phys. Lett. 356, 347-354.
    • (2002) Chem. Phys. Lett. , vol.356 , pp. 347-354
    • Gensch, T.1    Gradinam, C.C.2    Van Stokkum, I.H.M.3    Hendriks, J.4    Hellingwerf, K.J.5    Van Grondelle, R.6
  • 11
    • 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
  • 13
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8 angstrom 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 angstrom 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
  • 14
    • 0034745934 scopus 로고    scopus 로고
    • Structure of the I-1 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 I-1 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
  • 15
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • Xie, A. H., 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.H.1    Kelemen, L.2    Hendriks, J.3    White, B.J.4    Hellingwerf, K.J.5    Hoff, W.D.6
  • 17
    • 0036086458 scopus 로고    scopus 로고
    • A microspectrophotometer for UV-visible absorption and fluorescence studies of protein crystals
    • Bourgeois, D., X. Vemede, V. Adam, E. Fioravanti and T. Ursby (2002) A microspectrophotometer for UV-visible absorption and fluorescence studies of protein crystals. J. Appl. Crystallogr. 35, 319-326.
    • (2002) J. Appl. Crystallogr. , vol.35 , pp. 319-326
    • Bourgeois, D.1    Vemede, X.2    Adam, V.3    Fioravanti, E.4    Ursby, T.5
  • 18
    • 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
  • 19
    • 0028868422 scopus 로고
    • Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives
    • Imamoto, Y., T. Ito, M. Kataoka and F. Tokunaga (1995) Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives. FEBS Lett. 374, 157-160.
    • (1995) FEBS Lett. , vol.374 , pp. 157-160
    • Imamoto, Y.1    Ito, T.2    Kataoka, M.3    Tokunaga, F.4
  • 21
    • 0033974163 scopus 로고    scopus 로고
    • Conformational substates in different crystal forms of photoactive yellow protein-correlation with theoretical and experimental flexibility
    • van Aalten, D. M. F., W. Crielaard, K. J. Hellingwerf and L. Joshua-Tor (2000) Conformational substates in different crystal forms of photoactive yellow protein-correlation with theoretical and experimental flexibility. Protein Sci. 9, 64-72.
    • (2000) Protein Sci. , vol.9 , pp. 64-72
    • Van Aalten, D.M.F.1    Crielaard, W.2    Hellingwerf, K.J.3    Joshua-Tor, L.4
  • 22
    • 0023028920 scopus 로고
    • Crystallographic characterization of a photoactive yellow protein with photochemistry similar to sensory rhodopsin
    • McRee, D. E., T. E. Meyer, M. A. Cusanovich, H. E. Parge and E. D. Getzoff (1986) Crystallographic characterization of a photoactive yellow protein with photochemistry similar to sensory rhodopsin. J. Biol. Chem. 261, 13850-13851.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13850-13851
    • McRee, D.E.1    Meyer, T.E.2    Cusanovich, M.A.3    Parge, H.E.4    Getzoff, E.D.5
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant, A., K. Edman, T. Ursby, E. Pebay-Peyroula, E. M. Landau and R. Neutze (2000) Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature 406, 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
  • 26
    • 0035790044 scopus 로고    scopus 로고
    • Spectroscopic characterization of bacteriorhodopsin's L-intermediate in 3D crystals cooled to 170 K
    • Royant, A., K. Edman, T. Ursby, E. Pebay-Peyroula, E. M. Landau and R. Neutze (2001) Spectroscopic characterization of bacteriorhodopsin's L-intermediate in 3D crystals cooled to 170 K. Photochem. Photobiol. 74, 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
    • 0032575766 scopus 로고    scopus 로고
    • Assessing the functionality of a membrane protein in a three-dimensional crystal
    • Heberle, J., G. Buldt, E. Koglin, J. P. Rosenbusch and E. M. Landau (1998) Assessing the functionality of a membrane protein in a three-dimensional crystal. J. Mol. Biol. 281, 587-592.
    • (1998) J. Mol. Biol. , vol.281 , pp. 587-592
    • Heberle, J.1    Buldt, G.2    Koglin, E.3    Rosenbusch, J.P.4    Landau, E.M.5
  • 28
    • 0035345448 scopus 로고    scopus 로고
    • Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
    • Balashov, S. P. and T. G. Ebrey (2001) Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures. Photochem. Photobiol. 73, 453-462.
    • (2001) Photochem. Photobiol. , vol.73 , pp. 453-462
    • Balashov, S.P.1    Ebrey, T.G.2
  • 29
    • 0025052669 scopus 로고
    • Quantum efficiencies of bacteriorhodopsin photochemical reactions
    • Xie, A. H. (1990) Quantum efficiencies of bacteriorhodopsin photochemical reactions. Biophys. J. 58, 1127-1132.
    • (1990) Biophys. J. , vol.58 , pp. 1127-1132
    • Xie, A.H.1
  • 30
    • 0018476075 scopus 로고
    • Photoreaction of trans-bacteriorhodopsin at liquid helium temperature
    • Iwasa, T., F. Tokunaga and T. Yoshizawa (1979) Photoreaction of trans-bacteriorhodopsin at liquid helium temperature. FEBS Lett. 101, 121-124.
    • (1979) FEBS Lett. , vol.101 , pp. 121-124
    • Iwasa, T.1    Tokunaga, F.2    Yoshizawa, T.3
  • 32
    • 0032574723 scopus 로고    scopus 로고
    • Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering
    • Reat, V., H. Patzelt, M. Ferrand, C. Pfister, D. Oesterhelt and G. Zaccai (1998) Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering. Proc. Natl. Acad. Sci. USA 95, 4970-4975.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4970-4975
    • Reat, V.1    Patzelt, H.2    Ferrand, M.3    Pfister, C.4    Oesterhelt, D.5    Zaccai, G.6
  • 33
    • 0027317263 scopus 로고
    • The photochemical reactions of sensory rhodopsin I are altered by its transducer
    • Spudich, E. N. and J. L. Spudich (1993) The photochemical reactions of sensory rhodopsin I are altered by its transducer. J. Biol. Chem. 268, 16095-16097.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16095-16097
    • Spudich, E.N.1    Spudich, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.