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Volumn 99, Issue 3, 2010, Pages 944-952

Acrylonitrile quenching of Trp phosphorescence in proteins: A probe of the internal flexibility of the globular fold

Author keywords

[No Author keywords available]

Indexed keywords

2-(3-INDOLYL)ETHYLPHENYL KETONE; ACRYLONITRILE; GLASS; INDOLE DERIVATIVE; N-ACETYLTRYPTOPHANAMIDE; PROPIOPHENONE DERIVATIVE; PROTEIN; SOLUTION AND SOLUBILITY; TRYPTOPHAN;

EID: 77955681451     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.05.022     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 39549122002 scopus 로고    scopus 로고
    • Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
    • Kale, S., G. Ulas, F. Jordan. 2008. Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Proc. Natl. Acad. Sci. USA. 105:1158-1163.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1158-1163
    • Kale, S.1    Ulas, G.2    Jordan, F.3
  • 2
    • 38949183943 scopus 로고    scopus 로고
    • Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules
    • Persson, E., and B. Halle. 2008. Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules. J. Am. Chem. Soc. 130:1774-1787.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1774-1787
    • Persson, E.1    Halle, B.2
  • 3
    • 57349109904 scopus 로고    scopus 로고
    • Biocatalyst activity in nonaqueous environments correlates with centisecond-range protein motions
    • Eppler, R. K., E. P. Hudson, D. S. Clark. 2008. Biocatalyst activity in nonaqueous environments correlates with centisecond-range protein motions. Proc. Natl. Acad. Sci. USA. 105:15672-15677.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15672-15677
    • Eppler, R.K.1    Hudson, E.P.2    Clark, D.S.3
  • 5
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K., and D. Kern. 2007. Dynamic personalities of proteins. Nature. 450:964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 6
    • 25444532318 scopus 로고    scopus 로고
    • Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings
    • Bouvignies, G., P. Bernadó, M. Blackledge. 2005. Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings. Proc. Natl. Acad. Sci. USA. 102: 13885-13890.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13885-13890
    • Bouvignies, G.1    Bernadó, P.2    Blackledge, M.3
  • 7
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz, J. R., and G. Weber. 1973. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry. 12:4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 8
    • 0024115724 scopus 로고
    • Quenching of room temperature protein phosphorescence by added small molecules
    • Calhoun, D. B., S. W. Englander, J. M. Vanderkooi. 1988. Quenching of room temperature protein phosphorescence by added small molecules. Biochemistry. 27:8466-8474.
    • (1988) Biochemistry , vol.27 , pp. 8466-8474
    • Calhoun, D.B.1    Englander, S.W.2    Vanderkooi, J.M.3
  • 9
    • 0021114740 scopus 로고
    • Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence
    • Calhoun, D. B., J. M. Vanderkooi, and S.W. Englander. 1983. Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry. 22:1533-1539.
    • (1983) Biochemistry , vol.22 , pp. 1533-1539
    • Calhoun, D.B.1    Vanderkooi, J.M.2    Englander, S.W.3
  • 10
    • 0032544957 scopus 로고    scopus 로고
    • Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold
    • Cioni, P., and G. B. Strambini. 1998. Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold. J. Am. Chem. Soc. 120:11749-11757.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11749-11757
    • Cioni, P.1    Strambini, G.B.2
  • 11
    • 0033609806 scopus 로고    scopus 로고
    • Pressure/temperature effects on protein flexibility from acrylamide quenching of protein phosphorescence
    • Cioni, P., and G. B. Strambini. 1999. Pressure/temperature effects on protein flexibility from acrylamide quenching of protein phosphorescence. J. Mol. Biol. 291:955-964.
    • (1999) J. Mol. Biol. , vol.291 , pp. 955-964
    • Cioni, P.1    Strambini, G.B.2
  • 12
    • 0000591693 scopus 로고
    • Room temperature phosphorescence and the dynamic aspects of protein structure
    • Saviotti, M. L., and W. C. Galley. 1974. Room temperature phosphorescence and the dynamic aspects of protein structure. Proc. Natl. Acad. Sci. USA. 71:4154-4158.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4154-4158
    • Saviotti, M.L.1    Galley, W.C.2
  • 13
    • 0023378095 scopus 로고
    • 2 and NO. Evidence for inflexible regions of protein structure
    • 2 and NO. Evidence for inflexible regions of protein structure. Biophys. J. 52:23-28.
    • (1987) Biophys. J. , vol.52 , pp. 23-28
    • Strambini, G.B.1
  • 14
    • 0033568619 scopus 로고    scopus 로고
    • Pressure-temperature effects on oxygen quenching of protein phosphorescence
    • Strambini, G. B., and P. Cioni. 1999. Pressure-temperature effects on oxygen quenching of protein phosphorescence. J. Am. Chem. Soc. 121:8337-8344.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8337-8344
    • Strambini, G.B.1    Cioni, P.2
  • 15
    • 68249115779 scopus 로고    scopus 로고
    • Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: Evidence of gated quencher penetration
    • Strambini, G. B., and M. Gonnelli. 2009. Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: evidence of gated quencher penetration. Biochemistry. 48:7482-7491.
    • (2009) Biochemistry , vol.48 , pp. 7482-7491
    • Strambini, G.B.1    Gonnelli, M.2
  • 16
    • 0001084033 scopus 로고
    • Topics in fluorescence spectroscopy
    • J. R. Lakowicz, editor. Plenum, New York
    • Vanderkooi, J. M. 1991. Topics in fluorescence spectroscopy. In Biochemical Applications. J. R. Lakowicz, editor. Plenum, New York. 113-116.
    • (1991) Biochemical Applications , pp. 113-116
    • Vanderkooi, J.M.1
  • 17
    • 59349115572 scopus 로고    scopus 로고
    • No effect of covalently linked poly(ethylene glycol) chains on protein internal dynamics
    • Gonnelli, M., and G. B. Strambini. 2009. No effect of covalently linked poly(ethylene glycol) chains on protein internal dynamics. Biochim. Biophys. Acta. 1794:569-576.
    • (2009) Biochim. Biophys. Acta. , vol.1794 , pp. 569-576
    • Gonnelli, M.1    Strambini, G.B.2
  • 18
    • 84985441083 scopus 로고
    • Sensitization of the phosphorescence of indole through intramolecular energy transfer from the triplet state of covalently linked acetophenone in rigid media at 77 k
    • Tamaki, T. 1981. Sensitization of the phosphorescence of indole through intramolecular energy transfer from the triplet state of covalently linked acetophenone in rigid media at 77 k. Photochem. Photobiol. 33:31-34.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 31-34
    • Tamaki, T.1
  • 19
    • 0024511736 scopus 로고
    • Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli
    • Karlsson, B. G., T. Pascher, L. G. Lundberg. 1989. Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli. FEBS Lett. 246:211-217.
    • (1989) FEBS Lett , vol.246 , pp. 211-217
    • Karlsson, B.G.1    Pascher, T.2    Lundberg, L.G.3
  • 20
    • 0017567209 scopus 로고
    • The role of the nicotinamide and adenine subsites in the negative cooperativity 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 cooperativity 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
  • 21
    • 0025252558 scopus 로고
    • Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome C551 and nitrite reductase
    • van de Kamp, M., M. C. Silvestrini, G. W. Canters. 1990. Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome C551 and nitrite reductase. Eur. J. Biochem. 194:109-118.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 109-118
    • Van De Kamp, M.1    Silvestrini, M.C.2    Canters, G.W.3
  • 22
    • 0001018839 scopus 로고
    • Phosphorescence from Trp-48 in Azurin - Influence of Cu(Ii), Cu(I), Ag(I), and Cd(Ii) at the Coordination Site
    • Strambini, G. B., and E. Gabellieri. 1991. Phosphorescence from Trp-48 in Azurin - Influence of Cu(Ii), Cu(I), Ag(I), and Cd(Ii) at the Coordination Site. J. Phys. Chem. 95:4352-4356.
    • (1991) J. Phys. Chem. , vol.95 , pp. 4352-4356
    • Strambini, G.B.1    Gabellieri, E.2
  • 24
    • 12944308817 scopus 로고    scopus 로고
    • The triplet-state lifetime of indole derivatives in aqueous solution
    • Strambini, G. B., B. A. Kerwin, M. Gonnelli. 2004. The triplet-state lifetime of indole derivatives in aqueous solution. Photochem. Photobiol. 80:462-470.
    • (2004) Photochem. Photobiol. , vol.80 , pp. 462-470
    • Strambini, G.B.1    Kerwin, B.A.2    Gonnelli, M.3
  • 26
    • 0028068112 scopus 로고
    • Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosphorescence
    • Cioni, P., E. Gabellieri, G. B. Strambini. 1994. Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosphorescence. Biophys. Chem. 52:25-34.
    • (1994) Biophys. Chem. , vol.52 , pp. 25-34
    • Cioni, P.1    Gabellieri, E.2    Strambini, G.B.3
  • 27
    • 0000821397 scopus 로고    scopus 로고
    • The correct use of "average" fluorescence parameters
    • Sillen, A., and Y. Engelborghs. 1998. The correct use of "average" fluorescence parameters. Photochem. Photobiol. 65:475-486.
    • (1998) Photochem. Photobiol. , vol.65 , pp. 475-486
    • Sillen, A.1    Engelborghs, Y.2
  • 28
    • 0345691904 scopus 로고
    • Diffusion-dependent and-independent collisional quenching of fluorescence and phosphorescence
    • Owen, C. S., and J. M. Vanderkooi. 1991. Diffusion-dependent and-independent collisional quenching of fluorescence and phosphorescence. Comm. Mol. Cell. Biophys. 7:235-257.
    • (1991) Comm. Mol. Cell. Biophys. , vol.7 , pp. 235-257
    • Owen, C.S.1    Vanderkooi, J.M.2
  • 29
    • 0025350276 scopus 로고
    • Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence
    • Vanderkooi, J. M., S.W. Englander, 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    Owen, C.S.3
  • 30
    • 0001532454 scopus 로고
    • Long-distance (25Å) electron transfer by triplet excited states in rigid media
    • Miller, J. R., W. Hartman, and S. J. Abrash. 1982. Long-distance (25Å) electron transfer by triplet excited states in rigid media. J. Am. Chem. Soc. 104:4296-4298.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4296-4298
    • Miller, J.R.1    Hartman, W.2    Abrash, S.J.3
  • 31
    • 0001186153 scopus 로고
    • Law governing the diminution of fluorescent power as a function of concentration
    • Perrin, F. 1924. Law governing the diminution of fluorescent power as a function of concentration. Compt. Rend. 178:1978-1980.
    • (1924) Compt. Rend. , vol.178 , pp. 1978-1980
    • Perrin, F.1
  • 32
    • 0028503659 scopus 로고
    • Distance-dependent fluorescence quenching of tryptophan by acrylamide
    • Lakowicz, J. R., B. Zelent, M. L. Johnson. 1994. Distance-dependent fluorescence quenching of tryptophan by acrylamide. Photochem. Photobiol. 60:205-214.
    • (1994) Photochem. Photobiol. , vol.60 , pp. 205-214
    • Lakowicz, J.R.1    Zelent, B.2    Johnson, M.L.3
  • 33
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus, R. A., and N. Sutin. 1985. Electron transfer in chemistry and biology. Biochim. Biophys. Acta. 811:265-322.
    • (1985) Biochim. Biophys. Acta. , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 34
    • 18244397526 scopus 로고
    • A theory of sensitized luminescence in solids
    • Dexter, D. L. 1953. A theory of sensitized luminescence in solids. J. Chem. Phys. 21:836-850.
    • (1953) J. Chem. Phys. , vol.21 , pp. 836-850
    • Dexter, D.L.1
  • 35
    • 0007208536 scopus 로고
    • Determination of electron transfer rate constants from data on tunneling to randomly distributed acceptors in a rigid medium
    • Huddlestone, R. K., and J. R. Miller. 1982. Determination of electron transfer rate constants from data on tunneling to randomly distributed acceptors in a rigid medium. J. Phys. Chem. 86:200-203.
    • (1982) J. Phys. Chem. , vol.86 , pp. 200-203
    • Huddlestone, R.K.1    Miller, J.R.2
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0015048038 scopus 로고
    • Thermal stability of horse liver alcohol dehydrogenase and its complexes
    • Theorell, H., and K. Tatemoto. 1971. Thermal stability of horse liver alcohol dehydrogenase and its complexes. Arch. Biochem. Biophys. 143:354-358.
    • (1971) Arch. Biochem. Biophys. , vol.143 , pp. 354-358
    • Theorell, H.1    Tatemoto, K.2
  • 40
    • 0023043213 scopus 로고
    • Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry: Evidence for copper selectivity
    • Engeseth, H. R., and D. R. McMillin. 1986. Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry: evidence for copper selectivity. Biochemistry. 25:2448-2455.
    • (1986) Biochemistry , vol.25 , pp. 2448-2455
    • Engeseth, H.R.1    McMillin, D.R.2
  • 41
    • 0032774903 scopus 로고    scopus 로고
    • Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry
    • Levashov, P., V. Orlov, N. Nagradova. 1999. Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry. Biochim. Biophys. Acta. 1433:294-306.
    • (1999) Biochim. Biophys. Acta. , vol.1433 , pp. 294-306
    • Levashov, P.1    Orlov, V.2    Nagradova, N.3
  • 42
    • 0021133071 scopus 로고
    • Effect of free energy on rates of electron transfer between molecules
    • Miller, J. R., J. V. Beitz, and K. R. Huddlestone. 1984. Effect of free energy on rates of electron transfer between molecules. J. Am. Chem. Soc. 106:5057-5068.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5057-5068
    • Miller, J.R.1    Beitz, J.V.2    Huddlestone, K.R.3
  • 43
    • 0001917250 scopus 로고
    • Topics in fluorescence spectroscopy
    • J. R. Lakowicz, editor. Plenum, New York
    • Eftink, M. R. 1991. Topics in fluorescence spectroscopy. In Principles. J. R. Lakowicz, editor. Plenum, New York. 53-126.
    • (1991) Principles , pp. 53-126
    • Eftink, M.R.1


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