메뉴 건너뛰기




Volumn 95, Issue 4, 2008, Pages 1902-1912

Balance between ultrafast parallel reactions in the green fluorescent protein has a structural origin

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 50349096091     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.129957     Document Type: Article
Times cited : (35)

References (32)
  • 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
    • 0033065308 scopus 로고    scopus 로고
    • Shedding light on the dark and weakly fluorescent states of green fluorescent proteins
    • Weber, W., V. Helms, J. A. McCammon, and P. W. Langhoff. 1999. Shedding light on the dark and weakly fluorescent states of green fluorescent proteins. Proc. Natl. Acad. Sci. USA. 96:6177-6182.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6177-6182
    • Weber, W.1    Helms, V.2    McCammon, J.A.3    Langhoff, P.W.4
  • 4
    • 24944498464 scopus 로고    scopus 로고
    • Structural events in the photocycle of green fluorescent protein
    • van Thor, J. J., G. Zanetti, K. Ronayne, and M. Towrie. 2005. Structural events in the photocycle of green fluorescent protein. J. Phys. Chem. B. 109:16099-16108.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16099-16108
    • van Thor, J.J.1    Zanetti, G.2    Ronayne, K.3    Towrie, M.4
  • 5
    • 25844509913 scopus 로고    scopus 로고
    • Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein
    • van Thor, J. J., G. Y. Georgiev, M. Towrie, and J. T. Sage. 2005. Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein. J. Biol. Chem. 280:33652-33659.
    • (2005) J. Biol. Chem , vol.280 , pp. 33652-33659
    • van Thor, J.J.1    Georgiev, G.Y.2    Towrie, M.3    Sage, J.T.4
  • 6
    • 14844302645 scopus 로고    scopus 로고
    • Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy
    • Stoner-Ma, D., A. A. Jaye, P. Matousek, M. Towrie, S. R. Meech, and P. J. Tonge. 2005. Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy. J. Am. Chem. Soc. 127:2864-2865.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 2864-2865
    • Stoner-Ma, D.1    Jaye, A.A.2    Matousek, P.3    Towrie, M.4    Meech, S.R.5    Tonge, P.J.6
  • 7
    • 33751300213 scopus 로고    scopus 로고
    • Proton relay reaction in green fluorescent protein (GFP): Polarization-resolved ultrafast vibrational spectroscopy of isotopically edited GFP
    • Stoner-Ma, D., E. H. Melief, J. Nappa, K. L. Ronayne, P. J. Tonge, and S. R. Meech. 2006. Proton relay reaction in green fluorescent protein (GFP): polarization-resolved ultrafast vibrational spectroscopy of isotopically edited GFP. J. Phys. Chem. B. 110:22009-22018.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 22009-22018
    • Stoner-Ma, D.1    Melief, E.H.2    Nappa, J.3    Ronayne, K.L.4    Tonge, P.J.5    Meech, S.R.6
  • 8
    • 0029757121 scopus 로고    scopus 로고
    • Ultrafast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., B. A. King, G. U. Bublitz, and S. G. Boxer. 1996. Ultrafast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. USA. 93:8362-8367.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 9
    • 33745075006 scopus 로고    scopus 로고
    • Charge transfer in green fluorescent protein
    • van Thor, J. J., and J. T. Sage. 2006. Charge transfer in green fluorescent protein. Photochem. Photobiol. Sci. 5:597-602.
    • (2006) Photochem. Photobiol. Sci , vol.5 , pp. 597-602
    • van Thor, J.J.1    Sage, J.T.2
  • 11
    • 0029647452 scopus 로고
    • Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 1995. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O. Science. 269:962-966.
    • (1995) Science , vol.269 , pp. 962-966
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 12
    • 0037142658 scopus 로고    scopus 로고
    • The orientation of CO in heme proteins determined by time-resolved mid-IR spectroscopy: Anisotropy correction for finite photolysis of an optically thick sample
    • Lim, M. 2002. The orientation of CO in heme proteins determined by time-resolved mid-IR spectroscopy: anisotropy correction for finite photolysis of an optically thick sample. Bull. Korean Chem. Soc. 23:865-871.
    • (2002) Bull. Korean Chem. Soc , vol.23 , pp. 865-871
    • Lim, M.1
  • 13
    • 0001397162 scopus 로고    scopus 로고
    • Discordant results on FeCO deformability in heme proteins reconciled by density functional theory
    • Spiro, T. G., and P. M. Kozlovski. 1998. Discordant results on FeCO deformability in heme proteins reconciled by density functional theory. J. Am. Chem. Soc. 120:4524-4525.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 4524-4525
    • Spiro, T.G.1    Kozlovski, P.M.2
  • 14
    • 0035913380 scopus 로고    scopus 로고
    • Vibrational spectroscopy and mode assignments for an analog of the green fluorescent protein chromophore
    • Esposito, A. P., P. Schellenberg, W. W. Parson, and P. J. Reid. 2001. Vibrational spectroscopy and mode assignments for an analog of the green fluorescent protein chromophore. J. Mol. Struct. 569:25-41.
    • (2001) J. Mol. Struct , vol.569 , pp. 25-41
    • Esposito, A.P.1    Schellenberg, P.2    Parson, W.W.3    Reid, P.J.4
  • 15
    • 0037072002 scopus 로고    scopus 로고
    • Isotopic labeling and normal-mode analysis of a model green fluorescent protein chromophore
    • He, X., A. F. Bell, and P. J. Tonge. 2002. Isotopic labeling and normal-mode analysis of a model green fluorescent protein chromophore. J. Phys. Chem. B. 106:6056-6066.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6056-6066
    • He, X.1    Bell, A.F.2    Tonge, P.J.3
  • 17
    • 0027207780 scopus 로고
    • Theory of photoselection by intense light pulses. Influence of reorientational dynamics and chemical kinetics on absorbance measurements
    • Ansari, A., and A. Szabo. 1993. Theory of photoselection by intense light pulses. Influence of reorientational dynamics and chemical kinetics on absorbance measurements. Biophys. J. 64:838-851.
    • (1993) Biophys. J , vol.64 , pp. 838-851
    • Ansari, A.1    Szabo, A.2
  • 18
    • 85031364739 scopus 로고    scopus 로고
    • Frisch, M. J, G. W. Trucks, H. B. Schlegel, G. E. Scuseria, M. A. Robb, J. R. Cheeseman, J. A. Montgomery Jr, T. Vreven, K. N. Kudin, J. C. Burant, J. M. Millam, S. S. Iyengar, J. Tomasi, V. Barone, B. Mennucci, M. Cossi, G. Scalmani, N. Rega, G. A. Petersson, H. Nakatsuji, M. Hada, M. Ehara, K. Toyota, R. Fukuda, J. Hasegawa, M. Ishida, T. Nakajima, Y. Honda, O. Kitao, H. Nakai, M. Klene, X. Li, J. E. Knox, H. P. Hratchian, J. B. Cross, V. Bakken, C. Adamo, J. Jaramillo, R. Gomperts, R. E. Stratmann, O. Yazyev, A. J. Austin, R. Cammi, C. Pomelli, J. W. Ochterski, P. Y. Ayala, K. Morokuma, G. A. Voth, P. Salvador, J. J. Dannenberg, V. G. Zakrzewski, S. Dapprich, A. D. Daniels, M. C. Strain, O. Farkas, D. K. Malick, A. D. Rabuck, K. Raghavachari, J. B. Foresman, J. V. Ortiz, Q. Cui, A. G. Baboul, S. Clifford, J. Cioslowski, B. B. Stefanov, G. Liu, A. Liashenko, P. Piskorz, I. Komaromi, R. L. Martin, D. J. Fox, T. Keith, M. A. Al-Laham, C. Y. Peng, A. Nanayakkara, M. Challacombe, P. M
    • Frisch, M. J., G. W. Trucks, H. B. Schlegel, G. E. Scuseria, M. A. Robb, J. R. Cheeseman, J. A. Montgomery Jr., T. Vreven, K. N. Kudin, J. C. Burant, J. M. Millam, S. S. Iyengar, J. Tomasi, V. Barone, B. Mennucci, M. Cossi, G. Scalmani, N. Rega, G. A. Petersson, H. Nakatsuji, M. Hada, M. Ehara, K. Toyota, R. Fukuda, J. Hasegawa, M. Ishida, T. Nakajima, Y. Honda, O. Kitao, H. Nakai, M. Klene, X. Li, J. E. Knox, H. P. Hratchian, J. B. Cross, V. Bakken, C. Adamo, J. Jaramillo, R. Gomperts, R. E. Stratmann, O. Yazyev, A. J. Austin, R. Cammi, C. Pomelli, J. W. Ochterski, P. Y. Ayala, K. Morokuma, G. A. Voth, P. Salvador, J. J. Dannenberg, V. G. Zakrzewski, S. Dapprich, A. D. Daniels, M. C. Strain, O. Farkas, D. K. Malick, A. D. Rabuck, K. Raghavachari, J. B. Foresman, J. V. Ortiz, Q. Cui, A. G. Baboul, S. Clifford, J. Cioslowski, B. B. Stefanov, G. Liu, A. Liashenko, P. Piskorz, I. Komaromi, R. L. Martin, D. J. Fox, T. Keith, M. A. Al-Laham, C. Y. Peng, A. Nanayakkara, M. Challacombe, P. M. W. Gill, B. Johnson, W. Chen, M. W. Wong, C. Gonzalez, and J. A. Pople. 2004. Gaussian 03, Revision C.02. Gaussian, Wallingford, CT.
  • 19
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth, A., and C. Zscherp. 2002. What vibrations tell us about proteins. Q. Rev. Biophys. 35:369-430.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 20
    • 0035822210 scopus 로고    scopus 로고
    • Resonance Raman scattering by the green fluorescent protein and an analogue of its chromophore
    • Schellenberg, P., E. Johnson, A. P. Esposito, P. J. Reid, and W. W. Parson. 2001. Resonance Raman scattering by the green fluorescent protein and an analogue of its chromophore. J. Phys. Chem. B. 105:5316-5322.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5316-5322
    • Schellenberg, P.1    Johnson, E.2    Esposito, A.P.3    Reid, P.J.4    Parson, W.W.5
  • 21
    • 33748386052 scopus 로고    scopus 로고
    • Correlation between the vibrational frequencies of the carboxylate group and the types of its coordination to a metal ion: An ab initio molecular orbital study
    • Nara, M., H. Torii, and M. Tasumi. 1996. Correlation between the vibrational frequencies of the carboxylate group and the types of its coordination to a metal ion: an ab initio molecular orbital study. J. Phys. Chem. 100:19812-19817.
    • (1996) J. Phys. Chem , vol.100 , pp. 19812-19817
    • Nara, M.1    Torii, H.2    Tasumi, M.3
  • 23
    • 33645460315 scopus 로고    scopus 로고
    • Potential energy landscape of the photoinduced multiple proton-transfer process in the green fluorescent protein: Classical molecular dynamics and multiconfigurational electronic structure calculations
    • Vendrell, O., R. Gelabert, M. Moreno, and J. M. Lluch. 2006. Potential energy landscape of the photoinduced multiple proton-transfer process in the green fluorescent protein: classical molecular dynamics and multiconfigurational electronic structure calculations. J. Am. Chem. Soc. 128:3564-3574.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3564-3574
    • Vendrell, O.1    Gelabert, R.2    Moreno, M.3    Lluch, J.M.4
  • 24
    • 33645515454 scopus 로고    scopus 로고
    • Mechanistic aspects of proton chain transfer: A computational study for the green fluorescent protein chromophore
    • Wang, S., and S. C. Smith. 2006. Mechanistic aspects of proton chain transfer: a computational study for the green fluorescent protein chromophore. J, Phys. Chem. B. 110:5084-5093.
    • (2006) J, Phys. Chem. B , vol.110 , pp. 5084-5093
    • Wang, S.1    Smith, S.C.2
  • 25
    • 14844284623 scopus 로고    scopus 로고
    • A concerted mechanism of proton transfer in green fluorescent protein. A theoretical study
    • Zhang, R., M. T. Nguyn, and A. Ceuleman. 2005. A concerted mechanism of proton transfer in green fluorescent protein. A theoretical study. Chem. Phys. Lett. 404:250-256.
    • (2005) Chem. Phys. Lett , vol.404 , pp. 250-256
    • Zhang, R.1    Nguyn, M.T.2    Ceuleman, A.3
  • 26
    • 0037022637 scopus 로고    scopus 로고
    • Proton shuttle in green fluorescent protein studied by dynamic simulations
    • Lill, M. A., and V. Helms. 2002. Proton shuttle in green fluorescent protein studied by dynamic simulations. Proc. Natl. Acad. Sci. USA. 99:2778-2781.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2778-2781
    • Lill, M.A.1    Helms, V.2
  • 27
    • 22144472527 scopus 로고    scopus 로고
    • Proton pathways in green fluorescence protein
    • Agmon, N. 2005. Proton pathways in green fluorescence protein. Biophys. J. 88:2452-2461.
    • (2005) Biophys. J , vol.88 , pp. 2452-2461
    • Agmon, N.1
  • 28
    • 34547423998 scopus 로고    scopus 로고
    • Kinetics of switchable proton escape from a proton-wire within green fluorescence protein
    • Agmon, N. 2007. Kinetics of switchable proton escape from a proton-wire within green fluorescence protein. J. Phys. Chem. B. 111:7870-7878.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7870-7878
    • Agmon, N.1
  • 29
    • 0037435610 scopus 로고    scopus 로고
    • Polarized absorption spectra of green fluorescent protein single crystals: Transition dipole moment directions
    • Rosell, F. I., and S. G. Boxer. 2003. Polarized absorption spectra of green fluorescent protein single crystals: transition dipole moment directions. Biochemistry. 42:177-183.
    • (2003) Biochemistry , vol.42 , pp. 177-183
    • Rosell, F.I.1    Boxer, S.G.2
  • 30
    • 37249047410 scopus 로고    scopus 로고
    • Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C): Quantitative analysis of FRET in YFP dimers
    • Shi, X., J. Basran, H. E. Seward, W. Childs, C. R. Bagshaw, and S. G. Boxer. 2007. Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C): quantitative analysis of FRET in YFP dimers. Biochemistry. 46:14403-14417.
    • (2007) Biochemistry , vol.46 , pp. 14403-14417
    • Shi, X.1    Basran, J.2    Seward, H.E.3    Childs, W.4    Bagshaw, C.R.5    Boxer, S.G.6
  • 31
    • 32244434435 scopus 로고    scopus 로고
    • Probing the decay coordinate of the green fluorescent protein: Arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra
    • Stavrov, S. S., K. M. Solntsev, L. M. Tolbert, and D. Huppert. 2006. Probing the decay coordinate of the green fluorescent protein: arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra. J. Am. Chem. Soc. 128:1540-1546.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1540-1546
    • Stavrov, S.S.1    Solntsev, K.M.2    Tolbert, L.M.3    Huppert, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.