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Volumn 73, Issue 1-2, 1998, Pages 53-75

Time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide

Author keywords

Fluorophore; Phosphorescence; Quencher

Indexed keywords

ACRYLAMIDE; IODIDE; N ACETYLTRYPTOPHAN;

EID: 0344734168     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(98)00137-9     Document Type: Article
Times cited : (42)

References (54)
  • 3
    • 0018881999 scopus 로고
    • Fluorescence spectroscopic investigations of the dynamic properties of proteins, membranes, and nucleic acids
    • J.R. Lakowicz, Fluorescence spectroscopic investigations of the dynamic properties of proteins, membranes, and nucleic acids. J. Biochem. Biophys. Methods. 2 (1980) 90-119.
    • (1980) J. Biochem. Biophys. Methods , vol.2 , pp. 90-119
    • Lakowicz, J.R.1
  • 4
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • M.R. Eftink, C. Ghiron, Fluorescence quenching studies with proteins. Anal. Biochem. 114 (1981) 199-227.
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.2
  • 5
    • 0001917250 scopus 로고
    • Fluorescence quenching: Theory and applications
    • J.R. Lakowicz (Ed.)
    • M.R. Eftink, Fluorescence quenching: theory and applications, in: J.R. Lakowicz (Ed.), Topics in Fluorescence Spectroscopy, Vol. 2 (1991) pp. 53-126
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 53-126
    • Eftink, M.R.1
  • 6
  • 7
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion
    • S.S. Lehrer, Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10 (1971) 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 8
    • 0024115724 scopus 로고
    • Quenching of room temperature protein phosphorescence by added small molecules
    • D.B. Calhoun, S.W. Englander, W.W. Wright, J.M. Vanderkooi, Quenching of room temperature protein phosphorescence by added small molecules. Biochemistry 27 (1988) 8466-8474.
    • (1988) Biochemistry , vol.27 , pp. 8466-8474
    • Calhoun, D.B.1    Englander, S.W.2    Wright, W.W.3    Vanderkooi, J.M.4
  • 9
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in protein on the nanosecond timescale
    • J.R. Lakowicz, G. Weber, Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in protein on the nanosecond timescale. Biochemistry 12 (1973) 4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 11
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
    • J.R. Lakowicz, G. Weber, Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12 (1973) 4161-4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 12
    • 0026097986 scopus 로고
    • Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching
    • J.R. Lakowicz, I. Gryczynski, H. Szmacinski, H. Cherek, N. Joshi, Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching. Eur. Biophys. J. 19 (1991) 125-140.
    • (1991) Eur. Biophys. J. , vol.19 , pp. 125-140
    • Lakowicz, J.R.1    Gryczynski, I.2    Szmacinski, H.3    Cherek, H.4    Joshi, N.5
  • 13
    • 0004247952 scopus 로고
    • Diffusive transport of oxygen through proteins and membranes quantified by fluorescence quenching
    • C. Ho et al. (Eds.)
    • J.R. Lakowicz, Diffusive transport of oxygen through proteins and membranes quantified by fluorescence quenching, in: C. Ho et al. (Eds.), Hemoglobin and Oxygen Binding, vol. 1., 1982, pp. 443-448.
    • (1982) Hemoglobin and Oxygen Binding , vol.1 , pp. 443-448
    • Lakowicz, J.R.1
  • 15
    • 0010593040 scopus 로고
    • Diffusion and concentration of oxygen in microheterogeneous systems. Evaluation from luminescence quenching data
    • E.B. Abuin, E.A. Lissi, Diffusion and concentration of oxygen in microheterogeneous systems. Evaluation from luminescence quenching data. Prog. Reaction Kinetics 16 (1991) 1-33.
    • (1991) Prog. Reaction Kinetics , vol.16 , pp. 1-33
    • Abuin, E.B.1    Lissi, E.A.2
  • 16
    • 0022848310 scopus 로고
    • 5 in vesicles with an asymmetric transbilayer distribution of brominated phosphatidylcholine
    • 5 in vesicles with an asymmetric transbilayer distribution of brominated phosphatidylcholine. J. Biol. Chem. 261 (1986) 6725-6729.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6725-6729
    • James, E.1    Zlotnick, A.2    Tennyson, J.3    Holloway, P.4
  • 18
    • 0001614931 scopus 로고
    • Kinetics of the diffusion controlled reactions: Transient effects in fluorescence quenching
    • T.L. Nemzek, W.R. Ware, Kinetics of the diffusion controlled reactions: transient effects in fluorescence quenching. J. Chem. Phys. 62 (1975) 477-489.
    • (1975) J. Chem. Phys. , vol.62 , pp. 477-489
    • Nemzek, T.L.1    Ware, W.R.2
  • 19
    • 0000761639 scopus 로고
    • Kinetics of partly diffusion controlled reactions: I. Transient and apparent transient effect in fluorescence quenching
    • J.C. Andre, M. Niclause, W.R. Ware, Kinetics of partly diffusion controlled reactions: I. Transient and apparent transient effect in fluorescence quenching. Chem. Phys. 28 (1978) 371-377.
    • (1978) Chem. Phys. , vol.28 , pp. 371-377
    • Andre, J.C.1    Niclause, M.2    Ware, W.R.3
  • 20
    • 0023655927 scopus 로고
    • Diffusion coefficients of quenchers in proteins from transient effects in the intensity decays
    • J.R. Lakowicz, N.B. Joshi, M.L. Johnson, H. Szmacinski, I. Gryczynski, Diffusion coefficients of quenchers in proteins from transient effects in the intensity decays. J. Biol. Chem. 162 (1987) 10907-10910.
    • (1987) J. Biol. Chem. , vol.162 , pp. 10907-10910
    • Lakowicz, J.R.1    Joshi, N.B.2    Johnson, M.L.3    Szmacinski, H.4    Gryczynski, I.5
  • 21
    • 0041044543 scopus 로고
    • Transient effects in fluorescence quenching measured by 2 GHz frequency-domain fluorometry
    • J.R. Lakowicz, M.L. Johnson, I. Gryczynski, N. Joshi, G. Laczko, Transient effects in fluorescence quenching measured by 2 GHz frequency-domain fluorometry. J. Phys. Chem. 19 (1987) 3277-3285.
    • (1987) J. Phys. Chem. , vol.19 , pp. 3277-3285
    • Lakowicz, J.R.1    Johnson, M.L.2    Gryczynski, I.3    Joshi, N.4    Laczko, G.5
  • 22
    • 0343167639 scopus 로고
    • Conformational differences of oxytocin and vasopressin as observed by fluorescence anisotropy decays and transient effects in collisional quenching of tyrosine fluorescence
    • I. Gryczynski, H. Szmacinski, G. Laczko, W. Wiczk, M.L. Johnson, J. Kusba, J.R. Lakowicz, Conformational differences of oxytocin and vasopressin as observed by fluorescence anisotropy decays and transient effects in collisional quenching of tyrosine fluorescence. J. Fluorescence 1 (1991) 163-176.
    • (1991) J. Fluorescence , vol.1 , pp. 163-176
    • Gryczynski, I.1    Szmacinski, H.2    Laczko, G.3    Wiczk, W.4    Johnson, M.L.5    Kusba, J.6    Lakowicz, J.R.7
  • 23
    • 21144460540 scopus 로고
    • Frequency-domain fluorescence spectroscopy; instrumentation and applications
    • J.R. Lakowicz, I. Gryczynski, Frequency-domain fluorescence spectroscopy; instrumentation and applications. Arabian J. Sci. Engr. 17 (1992) 261-286.
    • (1992) Arabian J. Sci. Engr. , vol.17 , pp. 261-286
    • Lakowicz, J.R.1    Gryczynski, I.2
  • 24
    • 0001186799 scopus 로고
    • Radiation boundary conditions in collisional quenching of fluorescence determination by frequency-domain fluorometry
    • N. Joshi, M.L. Johnson, I. Gryczynski, J.R. Lakowicz, Radiation boundary conditions in collisional quenching of fluorescence determination by frequency-domain fluorometry. Chem. Phys. Lett. 135 (1987) 200-207.
    • (1987) Chem. Phys. Lett. , vol.135 , pp. 200-207
    • Joshi, N.1    Johnson, M.L.2    Gryczynski, I.3    Lakowicz, J.R.4
  • 27
    • 0010170523 scopus 로고
    • Distance-dependent quenching of Anthracene fluorescence by N,N-diethylaniline observed by frequency-domain flourometry
    • B. Zelent, J. Kuśba, I. Gryczynski, J.R. Lakowicz, Distance-dependent quenching of Anthracene fluorescence by N,N-diethylaniline observed by frequency-domain flourometry. Appl. Spectroscopy 43 (1995) 43-50.
    • (1995) Appl. Spectroscopy , vol.43 , pp. 43-50
    • Zelent, B.1    Kuśba, J.2    Gryczynski, I.3    Lakowicz, J.R.4
  • 28
    • 0000146432 scopus 로고    scopus 로고
    • Distance-dependent fluorescence quenching of p-bis[2-(5-phenyloxazolyl)]benzene by various quenchers
    • B. Zelent, J. Kuśba, I. Gryczynski, M.L. Johnson, J.R. Lakowicz, Distance-dependent fluorescence quenching of p-bis[2-(5-phenyloxazolyl)]benzene by various quenchers. J. Phys. Chem. 47 (1996) 18592-18602.
    • (1996) J. Phys. Chem. , vol.47 , pp. 18592-18602
    • Zelent, B.1    Kuśba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 32
    • 36549099529 scopus 로고
    • A subpicosecond, subnanosecond and steady-state study of diffusion-influenced fluorescence quenching
    • D.D. Eads, B.G. Dismer, G.R. Fleming, A subpicosecond, subnanosecond and steady-state study of diffusion-influenced fluorescence quenching. J. Chem. Phys. 93 (1990) 1136-1148.
    • (1990) J. Chem. Phys. , vol.93 , pp. 1136-1148
    • Eads, D.D.1    Dismer, B.G.2    Fleming, G.R.3
  • 33
    • 5644266542 scopus 로고
    • Temporal behavior of the rate for short-range energy transfer in fluid solution
    • J. Kuśba, B. Sipp, Temporal behavior of the rate for short-range energy transfer in fluid solution. Chem. Phys. 124 (1988) 223-226.
    • (1988) Chem. Phys. , vol.124 , pp. 223-226
    • Kuśba, J.1    Sipp, B.2
  • 34
    • 0028672836 scopus 로고
    • Diffusion modulated energy transfer and quenching: Analysis by numerical integration of the diffusion equation in la Place space
    • M.L. Johnson, L. Brand (Eds.), Academic Press, Inc., New York
    • J. Kuśba, J.R. Lakowicz, Diffusion modulated energy transfer and quenching: analysis by numerical integration of the diffusion equation in La Place space, in: M.L. Johnson, L. Brand (Eds.), Methods in Enzymology, Numerical Computer Methods, Pt. B, vol. 240, Academic Press, Inc., New York, 1994, pp. 216-262.
    • (1994) Methods in Enzymology, Numerical Computer Methods , vol.240 , Issue.PART B , pp. 216-262
    • Kuśba, J.1    Lakowicz, J.R.2
  • 35
    • 0022068786 scopus 로고
    • On the use of analytical approximate expressions for the transfer rate in excitation transfer kinetics
    • J. Kuśba, B. Sipp, On the use of analytical approximate expressions for the transfer rate in excitation transfer kinetics. J. Luminescence 33 (1985) 255-260.
    • (1985) J. Luminescence , vol.33 , pp. 255-260
    • Kuśba, J.1    Sipp, B.2
  • 36
    • 0000276617 scopus 로고    scopus 로고
    • Distance-dependent quenching of Nile Blue fluorescence by N,N-diethylaniline observed by frequency-domain fluorometry
    • J.R. Lakowicz, B. Zelent, J. Kuśba, I. Gryczynski, Distance-dependent quenching of Nile Blue fluorescence by N,N-diethylaniline observed by frequency-domain fluorometry. J. Fluorescence 6 (1996) 187-194.
    • (1996) J. Fluorescence , vol.6 , pp. 187-194
    • Lakowicz, J.R.1    Zelent, B.2    Kuśba, J.3    Gryczynski, I.4
  • 37
    • 0000335117 scopus 로고
    • The global analysis of fluorescence intensity and anisotropy decay data: Second-generation theory and programs
    • J.R. Lakowicz (Ed.), Plenum Press, New York
    • J.M. Beechem, E. Gratton, M. Ameloot, J.R. Knutson, L. Brand, The global analysis of fluorescence intensity and anisotropy decay data: second-generation theory and programs, in: J.R. Lakowicz (Ed.), Topics in Fluorescence Spectroscopy: Principles, vol. 2, Plenum Press, New York, 1991, pp. 241-305.
    • (1991) Topics in Fluorescence Spectroscopy: Principles , vol.2 , pp. 241-305
    • Beechem, J.M.1    Gratton, E.2    Ameloot, M.3    Knutson, J.R.4    Brand, L.5
  • 40
    • 1642549173 scopus 로고
    • Molecular volumes and Stokes-Einstein equation
    • J.T. Edward, Molecular volumes and Stokes-Einstein equation. J. Chem. Educ. 47 (1970) 261-270.
    • (1970) J. Chem. Educ. , vol.47 , pp. 261-270
    • Edward, J.T.1
  • 41
    • 84981677071 scopus 로고
    • Flash photolysis of N-acetyl-L-tryptophanamide: The relationship between radical yields and fluorescence quenching
    • R.F. Evans, R.R. Kuntz, W.A. Volkert, C.A. Ghiron, Flash photolysis of N-acetyl-L-tryptophanamide: the relationship between radical yields and fluorescence quenching. Photochem. Photobiol. 27 (1978) 511-515.
    • (1978) Photochem. Photobiol. , vol.27 , pp. 511-515
    • Evans, R.F.1    Kuntz, R.R.2    Volkert, W.A.3    Ghiron, C.A.4
  • 42
    • 84989712905 scopus 로고
    • The photophysics and photochemstry of the near-UV absorbing amino acids - I. Tryptophan and its simple derivatives
    • D. Creed, The photophysics and photochemstry of the near-UV absorbing amino acids - I. Tryptophan and its simple derivatives. Photochem. Photobiol. 39 (1984) 537-562.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 537-562
    • Creed, D.1
  • 43
    • 0001343498 scopus 로고
    • Nature, identification and properties of intermediates produced by UV excitation of indole derivatives at low and room temperatures. Some applicatons to tryptophan-containing proteins
    • R. Santus, M. Bazin, M. Aubailly, Nature, identification and properties of intermediates produced by UV excitation of indole derivatives at low and room temperatures. Some applicatons to tryptophan-containing proteins. Rev. Chem. Intermed. 3 (1980) 231-283.
    • (1980) Rev. Chem. Intermed. , vol.3 , pp. 231-283
    • Santus, R.1    Bazin, M.2    Aubailly, M.3
  • 44
    • 0030477430 scopus 로고    scopus 로고
    • Photoionization of indole, N-methylindole and tryptophan in aqueous solution upon excitation at 193 nm
    • W.G. McGimpsey, H. Görner, Photoionization of indole, N-methylindole and tryptophan in aqueous solution upon excitation at 193 nm. Photochem. Photobiol. 64 (1996) 501-509.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 501-509
    • McGimpsey, W.G.1    Görner, H.2
  • 45
    • 0345261443 scopus 로고
    • Fluorescence quenching due to the electron transfer. Indole-chloromethanes in rigid ethanol glass
    • A. Namiki, N. Nakashima, K. Yoshihara, Fluorescence quenching due to the electron transfer. Indole-chloromethanes in rigid ethanol glass. J. Chem. Phys. 71 (1979) 925-930.
    • (1979) J. Chem. Phys. , vol.71 , pp. 925-930
    • Namiki, A.1    Nakashima, N.2    Yoshihara, K.3
  • 46
    • 0000410853 scopus 로고
    • Contact and solvent-separated radical ion pairs in organic photochemistry
    • Springer-Verlag, Berlin, Heidelberg
    • J. Mattay, M. Vondenhof, Contact and solvent-separated radical ion pairs in organic photochemistry, Topics in Current Chemistry, Springer-Verlag, Berlin, Heidelberg, Vol. 159 (1991) 219-255.
    • (1991) Topics in Current Chemistry , vol.159 , pp. 219-255
    • Mattay, J.1    Vondenhof, M.2
  • 47
    • 0002301498 scopus 로고
    • Fundamental concepts of photoinduced electron transfer
    • Springer-Verlag, Berlin, Heidelberg
    • G.J. Kavarnos, Fundamental concepts of photoinduced electron transfer, Topics in Current Chemistry, Springer-Verlag, Berlin, Heidelberg, Vol. 156 (1990) 21-58.
    • (1990) Topics in Current Chemistry , vol.156 , pp. 21-58
    • Kavarnos, G.J.1
  • 48
    • 0002712816 scopus 로고
    • The Marcus inverted region
    • Springer-Verlag, Berlin, Heidelberg
    • P. Suppan, The Marcus inverted region, Topics in Current Chemistry, Springer-Verlag, Berlin, Heidelberg, Vol. 163 (1992) 95-130.
    • (1992) Topics in Current Chemistry , vol.163 , pp. 95-130
    • Suppan, P.1
  • 49
    • 0242485808 scopus 로고
    • Effects of external heavy atoms and other factors on the room-temperature phosphorescence and fluorescence of tryptophan and tyrosine
    • M.L. Meyers, P.G. Seybold, Effects of external heavy atoms and other factors on the room-temperature phosphorescence and fluorescence of tryptophan and tyrosine. Anal. Chem. 51 (1979) 1609-1612.
    • (1979) Anal. Chem. , vol.51 , pp. 1609-1612
    • Meyers, M.L.1    Seybold, P.G.2
  • 50
    • 0345337451 scopus 로고
    • Singlet and triplet quenching of indole by heavy atom containing molecules in a low temperature glassy matrix. Evidence for complexation in the triplet state
    • G. Lessard, G. Durocher, Singlet and triplet quenching of indole by heavy atom containing molecules in a low temperature glassy matrix. Evidence for complexation in the triplet state. J. Phys. Chem. 82 (1978) 2812-2819.
    • (1978) J. Phys. Chem. , vol.82 , pp. 2812-2819
    • Lessard, G.1    Durocher, G.2
  • 51
    • 0242581343 scopus 로고
    • Room temperature phosphorescence analysis; use of the external heavy-atom effect
    • P.G. Seybold, W. White, Room temperature phosphorescence analysis; use of the external heavy-atom effect. Anal. Chem. 47 (1975) 1199-1200.
    • (1975) Anal. Chem. , vol.47 , pp. 1199-1200
    • Seybold, P.G.1    White, W.2
  • 52
    • 0000344064 scopus 로고
    • Mechanisms of fluorescence quenching of aromatic molecules by potassium iodide and potassium bromide in methanol-ethanol solutions
    • J. Najbar, M. Mac, Mechanisms of fluorescence quenching of aromatic molecules by potassium iodide and potassium bromide in methanol-ethanol solutions. J. Chem. Soc. Faraday Trans. 87 (1991) 1523-1529.
    • (1991) J. Chem. Soc. Faraday Trans. , vol.87 , pp. 1523-1529
    • Najbar, J.1    Mac, M.2
  • 53
    • 0242665312 scopus 로고
    • External heavy-atom effect on the room-temperature luminescence of adsorbed dyes
    • W. White, P.G. Seybold, External heavy-atom effect on the room-temperature luminescence of adsorbed dyes. J. Phys. Chem. 81 (1977) 2035-2040.
    • (1977) J. Phys. Chem. , vol.81 , pp. 2035-2040
    • White, W.1    Seybold, P.G.2
  • 54
    • 0001018071 scopus 로고
    • Empirical study of heavy-atom collisonal quenching of the fluorescence state of aromatic compounds in solution
    • I.B. Berlman, Empirical study of heavy-atom collisonal quenching of the fluorescence state of aromatic compounds in solution. J. Phys. Chem. 77 (1973) 562-567.
    • (1973) J. Phys. Chem. , vol.77 , pp. 562-567
    • Berlman, I.B.1


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