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Volumn 44, Issue 14, 2005, Pages 5510-5524

Protonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C): A unifying mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CARBOXYLATION; FLOW MEASUREMENT; FLUORESCENCE; PHOTOCHEMICAL REACTIONS; RADIATION; SPECTROSCOPIC ANALYSIS;

EID: 20144386899     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047581f     Document Type: Article
Times cited : (96)

References (43)
  • 1
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein, Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 2
    • 0029757121 scopus 로고    scopus 로고
    • Ultrafast excited-state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., King, B. A., Bublitz, G. U., and Boxer, S. G. (1996) Ultrafast excited-state dynamics in green fluorescent protein: multiple states and proton transfer, Proc. Nat. Acad. Sci. U.S.A. 93, 8362-8367.
    • (1996) Proc. Nat. Acad. Sci. U.S.A. , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 3
    • 0036142426 scopus 로고    scopus 로고
    • Red-shifted mutants of green fluorescent protein: Reversible photoconversions studied by hole-burning and high-resolution spectroscopy
    • Creemers, T. M. H., Lock, A. J., Subramaniam, V., Jovin, T. M., and Volker, S. (2002) Red-shifted mutants of green fluorescent protein: reversible photoconversions studied by hole-burning and high-resolution spectroscopy, Chem. Phys. 275, 109-121.
    • (2002) Chem. Phys. , vol.275 , pp. 109-121
    • Creemers, T.M.H.1    Lock, A.J.2    Subramaniam, V.3    Jovin, T.M.4    Volker, S.5
  • 4
    • 0034602653 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy reveals fast optical excitation- driven intramolecular dynamics of yellow fluorescent proteins
    • Schwille, P., Kummer, S., Heikal, A. A., Moerner, W. E., and Webb, W. W. (2000) Fluorescence correlation spectroscopy reveals fast optical excitation- driven intramolecular dynamics of yellow fluorescent proteins, Proc. Natl. Acad. Sci. U.S.A. 97, 151-156.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 151-156
    • Schwille, P.1    Kummer, S.2    Heikal, A.A.3    Moerner, W.E.4    Webb, W.W.5
  • 5
    • 0000785746 scopus 로고    scopus 로고
    • Single molecule spectroscopy of the green fluorescent protein: A critical assessment
    • Zumbusch, A., and Jung, G. (2000) Single molecule spectroscopy of the green fluorescent protein: a critical assessment, Single Molecules 1, 261-270.
    • (2000) Single Molecules , vol.1 , pp. 261-270
    • Zumbusch, A.1    Jung, G.2
  • 6
    • 0030832226 scopus 로고    scopus 로고
    • On/off blinking and switching behaviour of single molecules of green fluorescent protein
    • Dickson, R. M., Cubitt, A. B., Tsien, R. Y., and Moerner, W. E. (1997) On/off blinking and switching behaviour of single molecules of green fluorescent protein, Nature 388, 355-358.
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 9
    • 0001218498 scopus 로고    scopus 로고
    • The fluorescence dynamics of single molecules of green fluorescent protein
    • Peterman, E. J. G., Brasselet, S., and Moerner, W. E. (1999) The fluorescence dynamics of single molecules of green fluorescent protein, J. Phys. Chem. A 103, 10553-10560.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 10553-10560
    • Peterman, E.J.G.1    Brasselet, S.2    Moerner, W.E.3
  • 10
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki, A., and Tsien, R. Y. (2000) Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein, Methods Enzymol. 327, 472-500.
    • (2000) Methods Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 12
    • 0034719112 scopus 로고    scopus 로고
    • Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: Implications for the open-closed transition identified by crystallography
    • Malnasi-Csizmadia, A., Woolley, R. J., and Bagshaw, C. R. (2000) Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: Implications for the open-closed transition identified by crystallography, Biochemistry 39, 16135-16146.
    • (2000) Biochemistry , vol.39 , pp. 16135-16146
    • Malnasi-Csizmadia, A.1    Woolley, R.J.2    Bagshaw, C.R.3
  • 13
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P. K., and Long, F. A. (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
  • 14
    • 0036713581 scopus 로고    scopus 로고
    • A novel pressure jump apparatus for the microvolume analysis of protein- ligand and protein-protein interactions: Application to nucleotide binding to skeletal and smooth muscle myosin subfragment 1
    • Pearson, D. S., Holtermann, G., Ellison, P., Cremo, C., and Geeves, M. A. (2002) A novel pressure jump apparatus for the microvolume analysis of protein- ligand and protein-protein interactions: Application to nucleotide binding to skeletal and smooth muscle myosin subfragment 1, Biochem. J. 15, 643-651.
    • (2002) Biochem. J. , vol.15 , pp. 643-651
    • Pearson, D.S.1    Holtermann, G.2    Ellison, P.3    Cremo, C.4    Geeves, M.A.5
  • 15
    • 0000575810 scopus 로고
    • Oscillations in the Spontaneous Fluorescence from Photosynthetic Reaction Centers
    • Stanley, R. J., and Boxer, S. G. (1995) Oscillations in the Spontaneous Fluorescence From Photosynthetic Reaction Centers, J. Phys. Chem. 99, 859-863.
    • (1995) J. Phys. Chem. , vol.99 , pp. 859-863
    • Stanley, R.J.1    Boxer, S.G.2
  • 16
    • 0000317426 scopus 로고    scopus 로고
    • Femtosecond spectroscopic study of relaxation processes of three amino-substituted coumarin dyes in methanol and dimethyl sulfoxide
    • Gustavsson, T., Cassara, L., Gulbinas, V., Gurzadyan, G., Mialocq, J. C., Pommeret, S., Sorgius, M., and van der Meulen, P. (1998) Femtosecond spectroscopic study of relaxation processes of three amino-substituted coumarin dyes in methanol and dimethyl sulfoxide, J. Phys. Chem. A 102, 4229-4245.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 4229-4245
    • Gustavsson, T.1    Cassara, L.2    Gulbinas, V.3    Gurzadyan, G.4    Mialocq, J.C.5    Pommeret, S.6    Sorgius, M.7    Van Der Meulen, P.8
  • 17
    • 0032435409 scopus 로고    scopus 로고
    • Measurement of ATPase activities of myosin at the level of tracks and single molecules
    • Conibear, P. B., Kuhlman, P. A., and Bagshaw, C. R. (1998) Measurement of ATPase activities of myosin at the level of tracks and single molecules, Adv. Exp. Med. Biol. 453, 15-26.
    • (1998) Adv. Exp. Med. Biol. , vol.453 , pp. 15-26
    • Conibear, P.B.1    Kuhlman, P.A.2    Bagshaw, C.R.3
  • 18
    • 0034536399 scopus 로고    scopus 로고
    • A comparison of optical geometries for combined flash photolysis and total internal reflection fluorescence microscopy
    • Conibear, P. B., and Bagshaw, C. R. (2000) A comparison of optical geometries for combined flash photolysis and total internal reflection fluorescence microscopy, J. Microsc. 200, 218-229.
    • (2000) J. Microsc. , vol.200 , pp. 218-229
    • Conibear, P.B.1    Bagshaw, C.R.2
  • 20
    • 0037328047 scopus 로고    scopus 로고
    • A prism combination for near isotropic fluorescence excitation by total internal reflection
    • Wakelin, S., and Bagshaw, C. R. (2003) A prism combination for near isotropic fluorescence excitation by total internal reflection, J. Microsc. 209, 143-148.
    • (2003) J. Microsc. , vol.209 , pp. 143-148
    • Wakelin, S.1    Bagshaw, C.R.2
  • 22
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • Wachter, R. M., Elsliger, M. A., Kallio, K., Hanson, G. T., and Remington, S. J. (1998) Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein, Structure 6, 1267-1277.
    • (1998) Structure , vol.6 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.A.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 23
    • 0033539088 scopus 로고    scopus 로고
    • Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate
    • Wachter, R. M., and Remington, S. J. (1999) Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate, Curr. Biol. 9, R628-R629.
    • (1999) Curr. Biol. , vol.9
    • Wachter, R.M.1    Remington, S.J.2
  • 24
    • 0037047334 scopus 로고    scopus 로고
    • Analysis of Nucleotide Binding to Dictyostelium Myosin II Motor Domains Containing a Single Tryptophan Near the Active Site
    • Kovacs, M., Malnasi-Csizmadia, A., Woolley, R. J., and Bagshaw, C. R. (2002) Analysis of Nucleotide Binding to Dictyostelium Myosin II Motor Domains Containing a Single Tryptophan Near the Active Site, J. Biol. Chem. 277, 28459-28467.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28459-28467
    • Kovacs, M.1    Malnasi-Csizmadia, A.2    Woolley, R.J.3    Bagshaw, C.R.4
  • 25
    • 0015446693 scopus 로고
    • Effects of pressure on the dissociation of weak acids
    • Disteche, A. (1972) Effects of pressure on the dissociation of weak acids, Symp. Soc. Exp. Biol. 26, 27-60.
    • (1972) Symp. Soc. Exp. Biol. , vol.26 , pp. 27-60
    • Disteche, A.1
  • 26
    • 0034053143 scopus 로고    scopus 로고
    • One- and two-photon excited fluorescence lifetimes and anisotropy decays of Green Fluorescent Proteins
    • Volkmer, A., Subramaniam, V., Birch, D. J. S., and Jovin, T. M. (2000) One- and two-photon excited fluorescence lifetimes and anisotropy decays of Green Fluorescent Proteins, Biophys. J. 78, 1589-1598.
    • (2000) Biophys. J. , vol.78 , pp. 1589-1598
    • Volkmer, A.1    Subramaniam, V.2    Birch, D.J.S.3    Jovin, T.M.4
  • 27
    • 0036140797 scopus 로고    scopus 로고
    • Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222
    • van Thor, J. J., Gensch, T., Hellingwerf, K. J., and Johnson, L. N. (2002) Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222, Nat. Struct. Biol. 9, 37-41.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 37-41
    • Van Thor, J.J.1    Gensch, T.2    Hellingwerf, K.J.3    Johnson, L.N.4
  • 29
    • 0000025962 scopus 로고
    • A Time-Resolved Fluorescence Study of Electronic Excitation- Energy Transport in Concentrated Dye Solutions
    • Scully, A. D., Matsumoto, A., and Hirayama, S. (1991) A Time-Resolved Fluorescence Study of Electronic Excitation- Energy Transport in Concentrated Dye Solutions, Chem. Phys. 157, 253-269.
    • (1991) Chem. Phys. , vol.157 , pp. 253-269
    • Scully, A.D.1    Matsumoto, A.2    Hirayama, S.3
  • 30
    • 0033065308 scopus 로고    scopus 로고
    • Shedding light on the dark and weakly fluorescent states of green fluorescent proteins
    • Weber, W., Helms, V., McCammon, J. A., and Langhoff, P. W. (1999) Shedding light on the dark and weakly fluorescent states of green fluorescent proteins, Proc. Natl. Acad. Sci. U.S.A. 96, 6177-6182.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6177-6182
    • Weber, W.1    Helms, V.2    McCammon, J.A.3    Langhoff, P.W.4
  • 31
    • 0034052719 scopus 로고    scopus 로고
    • Mechanism and cellular applications of a green fluorescent protein-based halide sensor
    • Jayaraman, S., Haggie, P., Wachter, R. M., Remington, S. J., and Verkman, A. S. (2000) Mechanism and cellular applications of a green fluorescent protein-based halide sensor, J. Biol. Chem. 275, 6047-6050.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6047-6050
    • Jayaraman, S.1    Haggie, P.2    Wachter, R.M.3    Remington, S.J.4    Verkman, A.S.5
  • 32
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen, M., Farinas, J., Li, Y., and Verkman, A. S. (1998) Green fluorescent protein as a noninvasive intracellular pH indicator, Biophys. J. 74, 1591-1599.
    • (1998) Biophys. J. , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 33
    • 0141749216 scopus 로고    scopus 로고
    • Kinetics of proton transfer in a green fluorescent protein: A laser-induced pH jump study
    • Mallik, R., Udgaonkar, J. B., and Krishnamoorthy, G. (2003) Kinetics of proton transfer in a green fluorescent protein: a laser-induced pH jump study, Proc. Indian Acad. Sci. 115, 307-317.
    • (2003) Proc. Indian Acad. Sci. , vol.115 , pp. 307-317
    • Mallik, R.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 34
    • 0032607868 scopus 로고    scopus 로고
    • Single-molecule fluorescence detection of green fluorescence protein and application to single-protein dynamics
    • Pierce, D. W., and Vale, R. D. (1999) Single-molecule fluorescence detection of green fluorescence protein and application to single-protein dynamics, Methods Cell Biol. 58, 49-73.
    • (1999) Methods Cell Biol. , vol.58 , pp. 49-73
    • Pierce, D.W.1    Vale, R.D.2
  • 35
    • 0030741606 scopus 로고    scopus 로고
    • Imaging individual green fluorescent proteins
    • Pierce, D. W., Hom-Booher, N., and Vale, R. D. (1997) Imaging individual green fluorescent proteins, Nature 388, 338.
    • (1997) Nature , vol.388 , pp. 338
    • Pierce, D.W.1    Hom-Booher, N.2    Vale, R.D.3
  • 36
    • 0016734139 scopus 로고
    • Partition analysis and the concept of net rate constants as tools in enzyme kinetics
    • Cleland, W. W. (1975) Partition analysis and the concept of net rate constants as tools in enzyme kinetics, Biochemistry 14, 3220-3224.
    • (1975) Biochemistry , vol.14 , pp. 3220-3224
    • Cleland, W.W.1
  • 37
    • 10844230260 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Taylor, K. B. (2002) Enzyme kinetics and mechanisms, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2002) Enzyme Kinetics and Mechanisms
    • Taylor, K.B.1
  • 38
    • 0000360525 scopus 로고
    • Structure of the Chromophore of Aequorea Green Fluorescent Protein
    • Shimomura, O. (1979) Structure of the Chromophore of Aequorea Green Fluorescent Protein, FEBS Lett. 104, 220-222.
    • (1979) FEBS Lett. , vol.104 , pp. 220-222
    • Shimomura, O.1
  • 40
    • 10044219858 scopus 로고    scopus 로고
    • Room temperature spectrally resolved single-molecule spectroscopy reveals new spectral forms and photophysical versatility of aequorea green fluorescent protein variants
    • Blum, C., Meixner, A. J., and Subramaniam, V. (2004) Room temperature spectrally resolved single-molecule spectroscopy reveals new spectral forms and photophysical versatility of aequorea green fluorescent protein variants, Biophys. J. 87, 4172-4179.
    • (2004) Biophys. J. , vol.87 , pp. 4172-4179
    • Blum, C.1    Meixner, A.J.2    Subramaniam, V.3
  • 43
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson, G. H., and Lippincott-Schwartz, J. (2002) A photoactivatable GFP for selective photolabeling of proteins and cells, Science 297, 1873-1877.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2


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