메뉴 건너뛰기




Volumn 84, Issue 2 I, 2003, Pages 1180-1191

Deuterium isotope effects in the photocycle transitions of the Photoactive Yellow Protein

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; PHOTOACTIVE YELLOW PROTEIN;

EID: 0037305871     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74932-7     Document Type: Article
Times cited : (54)

References (42)
  • 1
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G. E., D. R. Williams, and E. D. Getzoff. 1995. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 34:6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 2
    • 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
  • 3
    • 0034620544 scopus 로고    scopus 로고
    • Protonation states and pH titration in the photocycle of photoactive yellow protein
    • Demchuk, E., U. K. Genick, T. T. Woo, E. D. Getzoff, and D. Bashford. 2000. Protonation states and pH titration in the photocycle of photoactive yellow protein. Biochemistry. 39:1100-1113.
    • (2000) Biochemistry , vol.39 , pp. 1100-1113
    • Demchuk, E.1    Genick, U.K.2    Woo, T.T.3    Getzoff, E.D.4    Bashford, D.5
  • 4
    • 0032809454 scopus 로고    scopus 로고
    • Femtosecond spectroscopic observations of initial intermediates in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila
    • Devanathan, S., A. Pacheco, L. Ujj, M. Cusanovich, G. Tollin, S. Lin, and N. Woodbury. 1999. Femtosecond spectroscopic observations of initial intermediates in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys. J. 77:1017-1023.
    • (1999) Biophys. J. , vol.77 , pp. 1017-1023
    • Devanathan, S.1    Pacheco, A.2    Ujj, L.3    Cusanovich, M.4    Tollin, G.5    Lin, S.6    Woodbury, N.7
  • 5
    • 0002419950 scopus 로고
    • Resolution of overlapping bands. Functions for simulating band shapes
    • Fraser, R. D. B., and E. Suzuki. 1969. Resolution of overlapping bands. Functions for simulating band shapes. Anal. Chem. 41:37-39.
    • (1969) Anal. Chem. , vol.41 , pp. 37-39
    • Fraser, R.D.B.1    Suzuki, E.2
  • 8
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 Å 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 Å 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
  • 9
    • 0037156178 scopus 로고    scopus 로고
    • The primary photoreaction of photoactive yellow protein (PYP): Anisotropy changes and excitation wavelength dependence
    • Gensch, T., C. C. Gradinaru, 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    Gradinaru, C.C.2    Van Stokkum, I.H.M.3    Hendriks, J.4    Hellingwerf, K.J.5    Van Grondelle, R.6
  • 10
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P. K., and F. A. Long. 1960. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64:188-190.
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 11
    • 0036681395 scopus 로고    scopus 로고
    • Signal transduction in the photoactive yellow protein. I1. Proton transfer initiates conformational changes
    • Groenhof, G., M. F. Lensink, H. J. Berendsen, and A. E. Mark. 2002. Signal transduction in the photoactive yellow protein. I1. Proton transfer initiates conformational changes. Prot. Struct. Funct. Gen. 48:212-219.
    • (2002) Prot. Struct. Funct. Gen. , vol.48 , pp. 212-219
    • Groenhof, G.1    Lensink, M.F.2    Berendsen, H.J.3    Mark, A.E.4
  • 12
    • 0036199841 scopus 로고    scopus 로고
    • Transient exposure of hydrophobic surface in the photoactive yellow protein monitored with nile red
    • Hendriks, J., T. Gensch, L. Hviid, M. A. van Der Horst, K. J. Hellingwerf, and J. J. van Thor. 2002. Transient exposure of hydrophobic surface in the photoactive yellow protein monitored with nile red. Biophys. J. 82:1632-1643.
    • (2002) Biophys. J. , vol.82 , pp. 1632-1643
    • Hendriks, J.1    Gensch, T.2    Hviid, L.3    Van Der Horst, M.A.4    Hellingwerf, K.J.5    Van Thor, J.J.6
  • 13
    • 0033580921 scopus 로고    scopus 로고
    • Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophila
    • Hendriks, J., W. D. Hoff, W. Crielaard, and K. J. Hellingwerf. 1999a. Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophila. J. Biol. Chem. 274:17655-17660.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17655-17660
    • Hendriks, J.1    Hoff, W.D.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 14
    • 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. van Stokkum, W. Crielaard, and K. J. Hellingwerf. 1999b. 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.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 16
    • 0031574147 scopus 로고    scopus 로고
    • Comparison of acid denaturation and light activation in the eubacterial blue-light receptor photoactive yellow protein
    • Hoff, W. D., I. H. M. Van Stokkum, J. Gural, and K. J. Hellingwerf. 1997. Comparison of acid denaturation and light activation in the eubacterial blue-light receptor photoactive yellow protein. Biochim. Biophys. Acta. B. 1322:151-162.
    • (1997) Biochim. Biophys. Acta B , vol.1322 , pp. 151-162
    • Hoff, W.D.1    Van Stokkum, I.H.M.2    Gural, J.3    Hellingwerf, K.J.4
  • 18
    • 0034636790 scopus 로고    scopus 로고
    • Water structural changes involved in the activation process of photoactive yellow protein
    • Kandori, H., T. Iwata, J. Hendriks, A. Maeda, and K. J. Hellingwerf. 2000. Water structural changes involved in the activation process of photoactive yellow protein. Biochemistry. 39:7902-7909.
    • (2000) Biochemistry , vol.39 , pp. 7902-7909
    • Kandori, H.1    Iwata, T.2    Hendriks, J.3    Maeda, A.4    Hellingwerf, K.J.5
  • 19
    • 0033168713 scopus 로고    scopus 로고
    • Hydrogen tunneling in biology
    • Kohen, A., and J. P. Klinman. 1999. Hydrogen tunneling in biology. Chem. Biol. 6:R191-R198.
    • (1999) Chem. Biol. , vol.6
    • Kohen, A.1    Klinman, J.P.2
  • 21
    • 0035977041 scopus 로고    scopus 로고
    • Mimic of photocycle by a protein folding reaction in photoactive yellow protein
    • Lee, B. C., P. A. Croonquist, and W. D. Hoff. 2001a. Mimic of photocycle by a protein folding reaction in photoactive yellow protein. J. Biol. Chem. 276:44481-44487.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44481-44487
    • Lee, B.C.1    Croonquist, P.A.2    Hoff, W.D.3
  • 23
    • 0034335322 scopus 로고    scopus 로고
    • Probing the primary event in the photocycle of photoactive yellow protein using photochemical hole-burning technique
    • Masciangioli. T., S. Devanathan, M. A. Cusanovich, G. Tollin, and M. A. el-Sayed. 2000. Probing the primary event in the photocycle of photoactive yellow protein using photochemical hole-burning technique. Photochem. Photobiol. 72:639-644.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 639-644
    • Masciangioli, T.1    Devanathan, S.2    Cusanovich, M.A.3    Tollin, G.4    El-Sayed, M.A.5
  • 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, I. 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, I.H.3    Cusanovich, M.A.4
  • 25
    • 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
  • 26
    • 0027462930 scopus 로고
    • A light-dependent branching-reaction in the photocycle of the yellow protein from Ectothiorhodospira-Halophila
    • Miller, A., H. Leigeber, W. D. Hoff. and K. J. Hellingwerf. 1993. A light-dependent branching-reaction in the photocycle of the yellow protein from Ectothiorhodospira-Halophila. Biochim. Biophys. Acta. 1141: 190-196.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 190-196
    • Miller, A.1    Leigeber, H.2    Hoff, W.D.3    Hellingwerf, K.J.4
  • 27
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer, J. L., K. A. Wager-Smith, S. A. Kay, and E. D. Getzoff. 1998. Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc. Natl. Acad. Sci. USA. 95:5884-5890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-5890
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 29
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8 Å 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 Å 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
  • 30
    • 0034640464 scopus 로고    scopus 로고
    • Calculation of isotope effects from first principles
    • Scheiner, S. 2000. Calculation of isotope effects from first principles. Biochim. Biophys. Acta. 1458:28-42.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 28-42
    • Scheiner, S.1
  • 31
    • 0035902354 scopus 로고    scopus 로고
    • Density functional study of the photoactive yellow protein's chromophore
    • Sergi, A., M. Gruning, M. Ferrario. and F. Buda. 2001. Density functional study of the photoactive yellow protein's chromophore. J. Phys. Chem. B. 105:4386-4391.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 4386-4391
    • Sergi, A.1    Gruning, M.2    Ferrario, M.3    Buda, F.4
  • 33
    • 0036708464 scopus 로고    scopus 로고
    • Structural change of site-directed mutants of PYP: New dynamics during pR state
    • Takeshita, K., Y. Imamoto, M. Kataoka, K. Mihara, F. Tokunaga, and M. Terazima, 2002a. Structural change of site-directed mutants of PYP: new dynamics during pR state, Biophys. J. 83:1567-1577.
    • (2002) Biophys. J. , vol.83 , pp. 1567-1577
    • Takeshita, K.1    Imamoto, Y.2    Kataoka, M.3    Mihara, K.4    Tokunaga, F.5    Terazima, M.6
  • 34
    • 0037022785 scopus 로고    scopus 로고
    • Thermodynamic and transport properties of intermediate states of the photocyclic reaction of photoactive yellow protein
    • Takeshita, K., Y. Imamoto, M. Kataoka, F. Tokunaga, and M. Terazima. 2002b. Thermodynamic and transport properties of intermediate states of the photocyclic reaction of photoactive yellow protein, Biochemistry. 41:3037-3048.
    • (2002) Biochemistry , vol.41 , pp. 3037-3048
    • Takeshita, K.1    Imamoto, Y.2    Kataoka, M.3    Tokunaga, F.4    Terazima, M.5
  • 35
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: Internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 36
    • 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
  • 37
    • 0037018561 scopus 로고    scopus 로고
    • Target analysis of the bacteriorhodopsin photocycle using a spectrotemporal model
    • van Stokkum, I. H. M., and R. H. Lozier. 2002. Target analysis of the bacteriorhodopsin photocycle using a spectrotemporal model. J. Phys. Chem. B. 106:3477-3485.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3477-3485
    • Van Stokkum, I.H.M.1    Lozier, R.H.2
  • 38
    • 0001302210 scopus 로고
    • Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence
    • Van Stokkum, I. H. M., T. Scherer, A. M. Brouwer, and J. W. Verhoeven. 1994. Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence. J. Phys. Chem. 98:852-866.
    • (1994) J. Phys. Chem. , vol.98 , pp. 852-866
    • Van Stokkum, I.H.M.1    Scherer, T.2    Brouwer, A.M.3    Verhoeven, J.W.4
  • 40
    • 0030446427 scopus 로고    scopus 로고
    • Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein
    • Xie, A., W. D. Hoff,A. R. Kroon, and K. J. Hellingwerf. 1996. Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein. Biochemistry. 35:14671-14678.
    • (1996) Biochemistry , vol.35 , pp. 14671-14678
    • Xie, A.1    Hoff, W.D.2    Kroon, A.R.3    Hellingwerf, K.J.4
  • 41
    • 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
  • 42
    • 0035846381 scopus 로고    scopus 로고
    • Spectral tuning of photoactive yellow protein. Theoretical and experimental analysis of medium effects on the absorption spectrum of the chromophore
    • Yoda, M., H. Houjou, Y. Inoue, and M. Sakurai. 2001. Spectral tuning of photoactive yellow protein. Theoretical and experimental analysis of medium effects on the absorption spectrum of the chromophore. J. Phys. Chem. B. 105:9887-9895.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 9887-9895
    • Yoda, M.1    Houjou, H.2    Inoue, Y.3    Sakurai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.