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Volumn 77, Issue 1, 2003, Pages 101-109

Ab Initio Quantum Chemical Investigation of the First Steps of the Photocycle of Phototropin: A Model Study

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FLAVINE MONONUCLEOTIDE; HYDROGEN; MEMBRANE PROTEIN; PHOTOTROPIN; PROTEIN SUBUNIT; RADICAL; SULFUR; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 2342652526     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2003)077<0101:AIQCIO>2.0.CO;2     Document Type: Article
Times cited : (68)

References (38)
  • 2
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala, E., P. W. Oeller, E. Liscum, I.-S. Han, E. Larsen and W. R. Briggs (1997) Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278, 2120-2130.
    • (1997) Science , vol.278 , pp. 2120-2130
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.-S.4    Larsen, E.5    Briggs, W.R.6
  • 3
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (NPH1): Binding sites for the chromophore flavin mononucleotide
    • Christie, J. M., M. Salomon, K. Nozue, M. Wada and W. R. Briggs (1999) LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (NPH1): binding sites for the chromophore flavin mononucleotide. Proc. Natl. Acad. Sci. USA 96, 8779-8783.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 4
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., J. M. Christie, E. Knieb, U. Lempert and W. R. Briggs (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 5
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S. and K. Moffat (2001) Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc. Natl. Acad. Sci. USA 98, 2995-3000.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 6
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S. and K. Moffat (2002) Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14, 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 10
    • 0037062577 scopus 로고    scopus 로고
    • Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the lov2 domain of the plant blue-light receptor phototropin 1
    • Swartz, T. E., P. J. Wenzel, S. B. Corchnoy, W. R. Briggs and R. A. Bogomolni (2002) Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the lov2 domain of the plant blue-light receptor phototropin 1. Biochemistry, 41, 7183-7189.
    • (2002) Biochemistry , vol.41 , pp. 7183-7189
    • Swartz, T.E.1    Wenzel, P.J.2    Corchnoy, S.B.3    Briggs, W.R.4    Bogomolni, R.A.5
  • 12
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. (1993) Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 13
    • 0030570285 scopus 로고    scopus 로고
    • Treatment of electronic excitations within the adiabatic approximation of time dependent density functional theory
    • Bauernschmitt, R. and R. Ahlrichs (1996) Treatment of electronic excitations within the adiabatic approximation of time dependent density functional theory. Chem. Phys. Lett. 256, 454-464.
    • (1996) Chem. Phys. Lett. , vol.256 , pp. 454-464
    • Bauernschmitt, R.1    Ahlrichs, R.2
  • 14
    • 0000287603 scopus 로고    scopus 로고
    • Molecular excitation energies to high-lying bound states from time-dependent density-functional theory: Characterization and correction of the time-dependent local density approximation ionization threshold
    • Casida, M. E., C. Jamorski, K. C. Casida and D. R. Salahub (1998) Molecular excitation energies to high-lying bound states from time-dependent density-functional theory: characterization and correction of the time-dependent local density approximation ionization threshold. J. Chem. Phys. 108, 4439-4449.
    • (1998) J. Chem. Phys. , vol.108 , pp. 4439-4449
    • Casida, M.E.1    Jamorski, C.2    Casida, K.C.3    Salahub, D.R.4
  • 15
    • 0032533083 scopus 로고    scopus 로고
    • An efficient implementation of time-dependent density-functional theory for the calculation of excitation energies of large molecules
    • Stratmann, R. E., G. E. Scuseria and M. J. Frisch (1998) An efficient implementation of time-dependent density-functional theory for the calculation of excitation energies of large molecules. J. Chem. Phys. 109, 8218-8224.
    • (1998) J. Chem. Phys. , vol.109 , pp. 8218-8224
    • Stratmann, R.E.1    Scuseria, G.E.2    Frisch, M.J.3
  • 17
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi, A., E. Polverini, B. Quest and W. Gärtner (2002) First evidence for phototropin-related blue-light receptors in prokaryotes. Biophys. J. 82, 2627-2634.
    • (2002) Biophys. J. , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 18
    • 84995185847 scopus 로고
    • Theoretical considerations of the electronic spectra of methyl flavins
    • Song, P.-S. (1969) Theoretical considerations of the electronic spectra of methyl flavins. Int. J. Quant. Chem. 3, 303-316.
    • (1969) Int. J. Quant. Chem. , vol.3 , pp. 303-316
    • Song, P.-S.1
  • 19
    • 0015497790 scopus 로고
    • Molecular luminescence studies of flavins. I. The excited states of flavins
    • Sun, M., T. A. Moore and P.-S. Song (1972) Molecular luminescence studies of flavins. I. The excited states of flavins. J. Am. Chem. Soc. 94, 1730-1740.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 1730-1740
    • Sun, M.1    Moore, T.A.2    Song, P.-S.3
  • 20
    • 84987063183 scopus 로고
    • The structure and properties of flavins: Molecular orbital study based on totally optimized geometries. I. Molecular geometry investigations
    • Hall, L. H., B. J. Orchard and S. K. Tripathy (1987) The structure and properties of flavins: molecular orbital study based on totally optimized geometries. I. Molecular geometry investigations. Int. J. Quant. Chem. 31, 195-216.
    • (1987) Int. J. Quant. Chem. , vol.31 , pp. 195-216
    • Hall, L.H.1    Orchard, B.J.2    Tripathy, S.K.3
  • 21
    • 84987084453 scopus 로고
    • The structure and properties of flavins: Molecular orbital study based on totally optimized geometries. II. Molecular orbital structure electron distribution
    • Hall, L. H., B. J. Orchard and S. K. Tripathy (1987) The structure and properties of flavins: molecular orbital study based on totally optimized geometries. II. Molecular orbital structure electron distribution. Int. J. Quant. Chem. 31, 217-242.
    • (1987) Int. J. Quant. Chem. , vol.31 , pp. 217-242
    • Hall, L.H.1    Orchard, B.J.2    Tripathy, S.K.3
  • 22
    • 0023658602 scopus 로고
    • Further consideration of flavin coenzyme biochemistry afforded by geometry-optimized molecular orbital calculations
    • Hall, L. H., M. L. Bowers and C. N. Durfor (1987) Further consideration of flavin coenzyme biochemistry afforded by geometry-optimized molecular orbital calculations. Biochemistry 26, 7401-7409.
    • (1987) Biochemistry , vol.26 , pp. 7401-7409
    • Hall, L.H.1    Bowers, M.L.2    Durfor, C.N.3
  • 23
    • 0001669148 scopus 로고
    • Ab initio molecular orbital studies of closed shell flavins
    • Platenkamp, R. J., M. H. Palmer and A. J. W. G. Visser (1987) Ab initio molecular orbital studies of closed shell flavins. Eur. Biophys. J. 14, 393-402.
    • (1987) Eur. Biophys. J. , vol.14 , pp. 393-402
    • Platenkamp, R.J.1    Palmer, M.H.2    Visser, A.J.W.G.3
  • 24
    • 0000517552 scopus 로고    scopus 로고
    • Semiempirical and ab initio study of closed shell derivatives of 10-methylisoalloxazine: A model of flavin redox states
    • Meyer, M., H. Hartwig and D. Schomburg (1996) Semiempirical and ab initio study of closed shell derivatives of 10-methylisoalloxazine: a model of flavin redox states. J. Mol. Struct. (Theochem.) 364, 139-149.
    • (1996) J. Mol. Struct. (Theochem.) , vol.364 , pp. 139-149
    • Meyer, M.1    Hartwig, H.2    Schomburg, D.3
  • 25
    • 0029903531 scopus 로고    scopus 로고
    • A theoretical study of the structures of flavin in different oxidation and protonation states
    • Zheng, Y.-J. and R. L. Ornstein (1996) A theoretical study of the structures of flavin in different oxidation and protonation states. J. Am. Chem. Soc. 118, 9402-9408.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9402-9408
    • Zheng, Y.-J.1    Ornstein, R.L.2
  • 26
    • 0000255148 scopus 로고    scopus 로고
    • Electronic properties of flavins: Implications on the reactivity and absorption properties of flavoproteins
    • Wouters, J., F. Durant, B. Champagne and J.-M. André (1997) Electronic properties of flavins: implications on the reactivity and absorption properties of flavoproteins. Int. J. Quant. Chem. 64, 721-733.
    • (1997) Int. J. Quant. Chem. , vol.64 , pp. 721-733
    • Wouters, J.1    Durant, F.2    Champagne, B.3    André, J.-M.4
  • 27
    • 84981006049 scopus 로고
    • Spektren und Strukturen der am Flavin-Redoxsystem beteiligten Partikeln
    • Dudley, K. H., A. Ehrenberg, P. Hemmerich and F. Müller (1964) Spektren und Strukturen der am Flavin-Redoxsystem beteiligten Partikeln. Helv. Chim. Acta 47, 1354-1383.
    • (1964) Helv. Chim. Acta , vol.47 , pp. 1354-1383
    • Dudley, K.H.1    Ehrenberg, A.2    Hemmerich, P.3    Müller, F.4
  • 28
    • 0025363920 scopus 로고
    • Use of site-directed triple mutant to trap intermediates: Demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase
    • Miller, S. M., V. Massey, D. Ballou, C. H. Williams, M. D. Distefano, M. J. Moore and C. T. Walsh (1990) Use of site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry, 29, 2831-2841.
    • (1990) Biochemistry , vol.29 , pp. 2831-2841
    • Miller, S.M.1    Massey, V.2    Ballou, D.3    Williams, C.H.4    Distefano, M.D.5    Moore, M.J.6    Walsh, C.T.7
  • 29
    • 0036584875 scopus 로고    scopus 로고
    • Spectroscopic characterization of flavin mononucleotide bound to LOV1 domain of phot1 from Chlamydomonas reinhardtii
    • Holzer, W., A. Penzkofer, M. Fuhrmann and P. Hegemann (2002) Spectroscopic characterization of flavin mononucleotide bound to LOV1 domain of phot1 from Chlamydomonas reinhardtii. Photochem. Photobiol. 75, 479-487.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 479-487
    • Holzer, W.1    Penzkofer, A.2    Fuhrmann, M.3    Hegemann, P.4
  • 30
    • 84980139639 scopus 로고
    • A fast reacting intermediate in flash excited flavin solution
    • Tegnér, L. and B. Holström (1966) A fast reacting intermediate in flash excited flavin solution. Photochem. Photobiol. 5, 223-226.
    • (1966) Photochem. Photobiol. , vol.5 , pp. 223-226
    • Tegnér, L.1    Holström, B.2
  • 31
    • 84989674918 scopus 로고
    • Decay kinetics of the triplet excited state of lumiflavin
    • Naman, S. A. and L. Tegnér (1986) Decay kinetics of the triplet excited state of lumiflavin. Photochem. Photobiol. 43, 331-333.
    • (1986) Photochem. Photobiol. , vol.43 , pp. 331-333
    • Naman, S.A.1    Tegnér, L.2
  • 32
    • 0002611230 scopus 로고    scopus 로고
    • One-electron photoreduction of flavin mononucleotide: Time-resolved resonance Raman and absorption study
    • Sakai, M. and H. Takahashi (1996) One-electron photoreduction of flavin mononucleotide: time-resolved resonance Raman and absorption study. J. Mol. Struct. (Theochem.) 379, 9-18.
    • (1996) J. Mol. Struct. (Theochem.) , vol.379 , pp. 9-18
    • Sakai, M.1    Takahashi, H.2
  • 33
    • 0343390984 scopus 로고    scopus 로고
    • Hydrogen abstraction by triplet flavins. I: Time-resolved multi-channel absorption spectra of flash-irradiated riboflavin solutions in water
    • Melø, T. B., M. A. Ionescu, G. W. Haggquist and K. R. Naqvi (1999) Hydrogen abstraction by triplet flavins. I: time-resolved multi-channel absorption spectra of flash-irradiated riboflavin solutions in water. Spectrochim. Acta Part A 55, 2299-2307.
    • (1999) Spectrochim. Acta Part A , vol.55 , pp. 2299-2307
    • Melø, T.B.1    Ionescu, M.A.2    Haggquist, G.W.3    Naqvi, K.R.4
  • 34
    • 0009975795 scopus 로고
    • Electron paramagnetic resonance studies of the triplet state of flavin and pteridine derivatives
    • Lhoste, J. M., A. Haug and P. Hemmerich (1966) Electron paramagnetic resonance studies of the triplet state of flavin and pteridine derivatives. Biochemistry 5, 3290-3300.
    • (1966) Biochemistry , vol.5 , pp. 3290-3300
    • Lhoste, J.M.1    Haug, A.2    Hemmerich, P.3
  • 35
    • 0014265295 scopus 로고
    • On the basicity of the excited state of flavins
    • Song, P.-S. (1968) On the basicity of the excited state of flavins. Photochem. Photobiol. 7, 311-313.
    • (1968) Photochem. Photobiol. , vol.7 , pp. 311-313
    • Song, P.-S.1
  • 36
    • 0016662393 scopus 로고
    • Determination of the pK values of the lumiflavin triplet state by flash photolysis
    • Schreiner, S., U. Steiner and H. E. A. Kramer (1975) Determination of the pK values of the lumiflavin triplet state by flash photolysis. Photochem. Photobiol. 21, 81-84.
    • (1975) Photochem. Photobiol. , vol.21 , pp. 81-84
    • Schreiner, S.1    Steiner, U.2    Kramer, H.E.A.3
  • 37
    • 21144484467 scopus 로고
    • Ab initio CI study of hydrogen abstraction from hydrogen and methyl sulfide by ketone triplet excited state
    • Cardy, H., E. Poquet, M. Chaillet and J. Ollivier (1993) Ab initio CI study of hydrogen abstraction from hydrogen and methyl sulfide by ketone triplet excited state. Chem. Phys. 173, 79-90.
    • (1993) Chem. Phys. , vol.173 , pp. 79-90
    • Cardy, H.1    Poquet, E.2    Chaillet, M.3    Ollivier, J.4
  • 38
    • 84981621777 scopus 로고
    • A laser flash photolysis study of the nature of flavin mononucleotide triplet states and the reactions of the neutral form with amino acids
    • Heelis, P. F., B. J. Parsons, G. O. Phillips and J. F. McKellar (1978) A laser flash photolysis study of the nature of flavin mononucleotide triplet states and the reactions of the neutral form with amino acids. Photochem. Photobiol. 28, 169-173.
    • (1978) Photochem. Photobiol. , vol.28 , pp. 169-173
    • Heelis, P.F.1    Parsons, B.J.2    Phillips, G.O.3    McKellar, J.F.4


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