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Volumn 74, Issue 6, 1998, Pages 3165-3172

Tyrosine quenching of tryptophan phosphorescence in glyceraidehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MUTANT PROTEIN; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

EID: 0031835675     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78022-1     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0016851391 scopus 로고
    • Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan
    • Bent, D. V., and E. Hayon. 1975. Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan. J. Am. Chem. Soc. 97:2612-2619.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 2612-2619
    • Bent, D.V.1    Hayon, E.2
  • 3
    • 0024364915 scopus 로고
    • Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectors
    • Cioni, P., and G. B. Strambini. 1989. Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectors. J. Mol. Biol. 207:237-247.
    • (1989) J. Mol. Biol. , vol.207 , pp. 237-247
    • Cioni, P.1    Strambini, G.B.2
  • 4
    • 0027934772 scopus 로고
    • Pressure effects on protein flexibility: Monomeric proteins
    • Cioni, P., and G. B. Strambini. 1994. Pressure effects on protein flexibility: monomeric proteins. J. Mol. Biol. 242:291-301.
    • (1994) J. Mol. Biol. , vol.242 , pp. 291-301
    • Cioni, P.1    Strambini, G.B.2
  • 5
    • 0030589135 scopus 로고    scopus 로고
    • Pressure effects on the structure of oligomeric proteins prior to subunit dissociation
    • Cioni, P., and G. B. Strambini. 1996. Pressure effects on the structure of oligomeric proteins prior to subunit dissociation. J. Mol. Biol. 263: 789-799.
    • (1996) J. Mol. Biol. , vol.263 , pp. 789-799
    • Cioni, P.1    Strambini, G.B.2
  • 6
    • 0029842117 scopus 로고    scopus 로고
    • + binding on the luminescence of tryptophans 84 and 310 of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • + binding on the luminescence of tryptophans 84 and 310 of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochemistry. 35:12549-12559.
    • (1996) Biochemistry , vol.35 , pp. 12549-12559
    • Gabellieri, E.1    Rahuel-Clermont, S.2    Branlant, G.3    Strambini, G.B.4
  • 7
    • 0028294925 scopus 로고
    • Conformational changes in proteins induced by dynamic associations. A tryptophan phosphorescence study
    • Gabellieri, E., and G. B. Strambini. 1994. Conformational changes in proteins induced by dynamic associations. A tryptophan phosphorescence study. Eur. J. Biochem. 221:77-85.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 77-85
    • Gabellieri, E.1    Strambini, G.B.2
  • 8
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: Evidence of ice-induced partial unfolding
    • Gabellieri, E., and G. B. Strambini. 1996. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys. J. 70:971-976.
    • (1996) Biophys. J. , vol.70 , pp. 971-976
    • Gabellieri, E.1    Strambini, G.B.2
  • 9
    • 0027254999 scopus 로고
    • Glycerol effects on protein flexibility: A tryptophan phosphorescence study
    • Gonnelli, M., and G. B. Strambini. 1993. Glycerol effects on protein flexibility: a tryptophan phosphorescence study. Biophys. J. 65:131-137.
    • (1993) Biophys. J. , vol.65 , pp. 131-137
    • Gonnelli, M.1    Strambini, G.B.2
  • 10
    • 0028866475 scopus 로고
    • Phosphorescence lifetime of tryptophan in proteins
    • Gonnelli, M., and G. B. Strambini. 1995. Phosphorescence lifetime of tryptophan in proteins. Biochemistry. 34:13847-13857.
    • (1995) Biochemistry , vol.34 , pp. 13847-13857
    • Gonnelli, M.1    Strambini, G.B.2
  • 11
    • 0002323195 scopus 로고
    • Protein hydration and glass transition behavior
    • R. B. Gregory, editor. Marcel Dekker, New York
    • Gregory, R. B. 1995. Protein hydration and glass transition behavior. In Protein Solvent Interactions. R. B. Gregory, editor. Marcel Dekker, New York. 191-264.
    • (1995) Protein Solvent Interactions , pp. 191-264
    • Gregory, R.B.1
  • 12
    • 0000348209 scopus 로고    scopus 로고
    • Lowest triplet state of indole: An ab initio study
    • Hahn, D. K., and P. R. Callis. 1997. Lowest triplet state of indole: an ab initio study. J. Phys. Chem. 101:2686-2691.
    • (1997) J. Phys. Chem. , vol.101 , pp. 2686-2691
    • Hahn, D.K.1    Callis, P.R.2
  • 13
    • 0029792732 scopus 로고    scopus 로고
    • Detection of a pH dependent conformational change in azurin by time-resolved phosphorescence
    • Hansen, J. E., D. G. Steel, and A. Gafni. 1996. Detection of a pH dependent conformational change in azurin by time-resolved phosphorescence. Biophys. J. 71:2138-2143.
    • (1996) Biophys. J. , vol.71 , pp. 2138-2143
    • Hansen, J.E.1    Steel, D.G.2    Gafni, A.3
  • 14
    • 0017567209 scopus 로고
    • The role of the nicotinamide and adenine subsites in the negative co-operativity of coenzyme binding to glyceraldehyde-3-phosphate dehydrogenase
    • Henis, Y. I., and A. Levitzki, 1977. The role of the nicotinamide and adenine subsites in the negative co-operativity of coenzyme binding to glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 117:699-716.
    • (1977) J. Mol. Biol. , vol.117 , pp. 699-716
    • Henis, Y.I.1    Levitzki, A.2
  • 15
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracyl-containing DNA
    • Kunkel, T. A., K. Bebenek, and J. McClary. 1991. Efficient site-directed mutagenesis using uracyl-containing DNA. Methods Enzymol. 204: 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 16
    • 0026780261 scopus 로고
    • Temperature dependence of the disulfide perturbation to the triplet state of tryptophan
    • Li, Z., A. Bruce, and W. C. Galley. 1992. Temperature dependence of the disulfide perturbation to the triplet state of tryptophan. Biophys. J. 61:1364-1371.
    • (1992) Biophys. J. , vol.61 , pp. 1364-1371
    • Li, Z.1    Bruce, A.2    Galley, W.C.3
  • 17
    • 0003022448 scopus 로고
    • Luminescence of polypeptides and proteins
    • R. F. Steiner and I. Weinryb, editors. Plenum Press, New York
    • Longworth, J. W. 1971. Luminescence of polypeptides and proteins. In The Excited States of Proteins and Nucleic Acids. R. F. Steiner and I. Weinryb, editors. Plenum Press, New York. 319-484.
    • (1971) The Excited States of Proteins and Nucleic Acids , pp. 319-484
    • Longworth, J.W.1
  • 18
    • 0031008248 scopus 로고    scopus 로고
    • Time-resolved room temperature tryptophan phosphorescence in proteins
    • Schauerte, J. A., D. G. Steel, and A. Gafni. 1997. Time-resolved room temperature tryptophan phosphorescence in proteins. Methods Enzymol. 278:49-71.
    • (1997) Methods Enzymol. , vol.278 , pp. 49-71
    • Schauerte, J.A.1    Steel, D.G.2    Gafni, A.3
  • 19
    • 0023717499 scopus 로고
    • Coenzyme induced conformational changes in glyceraldehyde-3-phopshate dehydrogenase from B. stearothermophilus
    • Skarzynski, T., and A. J. Wonacott. 1988. Coenzyme induced conformational changes in glyceraldehyde-3-phopshate dehydrogenase from B. stearothermophilus. J. Mol. Biol. 203:1097-1118.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1097-1118
    • Skarzynski, T.1    Wonacott, A.J.2
  • 20
    • 0027176877 scopus 로고
    • Temperature dependence of the phosphorescence quantum yield of various α-lactalbumins and of hen egg-white lysozyme
    • Smith, C. A., and A. H. Maki. 1993. Temperature dependence of the phosphorescence quantum yield of various α-lactalbumins and of hen egg-white lysozyme. Biophys. J. 64:1885-1895.
    • (1993) Biophys. J. , vol.64 , pp. 1885-1895
    • Smith, C.A.1    Maki, A.H.2
  • 21
    • 0002481190 scopus 로고
    • Tryptophan phosphorescence as a monitor of protein flexibility
    • Strambini, G. B. 1989. Tryptophan phosphorescence as a monitor of protein flexibility. J. Mol. Liq. 42:155-165.
    • (1989) J. Mol. Liq. , vol.42 , pp. 155-165
    • Strambini, G.B.1
  • 22
    • 0021452281 scopus 로고
    • Intrinsic phosphorescence from proteins in the solid state
    • Strambini, G. B., and E. Gabellieri. 1984. Intrinsic phosphorescence from proteins in the solid state. Photochem. Photobiol. 39:725-729.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 725-729
    • Strambini, G.B.1    Gabellieri, E.2
  • 23
    • 0023646714 scopus 로고
    • Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domain
    • Strambini, G. B., and E. Gabellieri. 1987. Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domain. Biochemistry. 26:6527-6530.
    • (1987) Biochemistry , vol.26 , pp. 6527-6530
    • Strambini, G.B.1    Gabellieri, E.2
  • 24
    • 0025440698 scopus 로고
    • Temperature dependence of tryptophan phosphorescence in proteins
    • Strambini, G. B., and E. Gabellieri. 1990. Temperature dependence of tryptophan phosphorescence in proteins. Photochem. Photobiol. 51:643-648.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 643-648
    • Strambini, G.B.1    Gabellieri, E.2
  • 25
    • 0000760481 scopus 로고
    • Quenching of indole by copper ions: A distance dependence study
    • Strambini, G. B., and E. Gabellieri. 1991. Quenching of indole by copper ions: a distance dependence study. J. Phys. Chem. 95:4347-4352.
    • (1991) J. Phys. Chem. , vol.95 , pp. 4347-4352
    • Strambini, G.B.1    Gabellieri, E.2
  • 26
    • 0000986668 scopus 로고
    • The indole nucleus triplet-state lifetime and its dependence on solvent microviscosity
    • Strambini, G. B., and M. Gonnelli. 1985. The indole nucleus triplet-state lifetime and its dependence on solvent microviscosity. Chem. Phys. Lett. 115:196-200.
    • (1985) Chem. Phys. Lett. , vol.115 , pp. 196-200
    • Strambini, G.B.1    Gonnelli, M.2
  • 27
    • 0023043182 scopus 로고
    • Effects of urea and guanidine hydrochloride on the activity and dynamical structure of equine liver alcohol dehydrogenase
    • Strambini, G. B., and M. Gonnelli. 1986. Effects of urea and guanidine hydrochloride on the activity and dynamical structure of equine liver alcohol dehydrogenase. Biochemistry. 25:2471-2476.
    • (1986) Biochemistry , vol.25 , pp. 2471-2476
    • Strambini, G.B.1    Gonnelli, M.2
  • 28
    • 0001185890 scopus 로고
    • Protein dynamical structure by tryptophan phosphorescence and enzymatic activity in reverse micelles. 1. Liver alcohol dehydrogenase
    • Strambini, G. B., and M. Gonnelli. 1988. Protein dynamical structure by tryptophan phosphorescence and enzymatic activity in reverse micelles. 1. Liver alcohol dehydrogenase. J. Phys. Chem. 92:2850-2853.
    • (1988) J. Phys. Chem. , vol.92 , pp. 2850-2853
    • Strambini, G.B.1    Gonnelli, M.2
  • 29
    • 0025097970 scopus 로고
    • Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme: A comparative study of protein conformation in solution
    • Strambini, G. B., and M. Gonnelli. 1990. Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme: a comparative study of protein conformation in solution. Biochemistry. 29: 196-203.
    • (1990) Biochemistry , vol.29 , pp. 196-203
    • Strambini, G.B.1    Gonnelli, M.2
  • 30
    • 0000145156 scopus 로고
    • Tryptophan phosphorescence in fluid solution
    • Strambini, G. B., and M. Gonnelli. 1995. Tryptophan phosphorescence in fluid solution. J. Am. Chem. Soc. 117:7646-7651.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7646-7651
    • Strambini, G.B.1    Gonnelli, M.2
  • 31
    • 0030948494 scopus 로고    scopus 로고
    • Room temperature phosphorescence study of phosphate binding in Escherichia coli alkaline phosphatase
    • Sun, L., E. R. Kantrowitz, and W. C. Galley. 1997. Room temperature phosphorescence study of phosphate binding in Escherichia coli alkaline phosphatase. Eur. J. Biochem. 245:32-39.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 32-39
    • Sun, L.1    Kantrowitz, E.R.2    Galley, W.C.3
  • 32
    • 0001084033 scopus 로고
    • Tryptophan phosphorescence from proteins at room temperature
    • J. R. Lakowicz, editor. Plenum Press, New York
    • Vanderkooi, J. M. 1992. Tryptophan phosphorescence from proteins at room temperature. In Topics in Fluorescence Spectroscopy. J. R. Lakowicz, editor. Plenum Press, New York. 113-136.
    • (1992) Topics in Fluorescence Spectroscopy , pp. 113-136
    • Vanderkooi, J.M.1
  • 33
    • 0025350276 scopus 로고
    • Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence
    • Vanderkooi, J. M., S. W. Englander, S. Papp, W. W. Wright, and C. S. Owen. 1990. Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proc. Natl. Acad. Sci. USA. 87:5099-5103.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5099-5103
    • Vanderkooi, J.M.1    Englander, S.W.2    Papp, S.3    Wright, W.W.4    Owen, C.S.5


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