Temperature dependence of tryptophan fluorescence lifetime in aqueous glycerol and trehalose solutions
Tóm tắt
The temperature dependences of tryptophan fluorescence decay kinetics in aqueous glycerol and 1 M trehalose solutions were examined. The fluorescence decay kinetics were recorded in the spectral region of 292.5–417.5 nm with nanosecond time resolution. The kinetics curves were approximated by the sum of three exponential terms, and the spectral distribution (DAS) of these components was determined. An antisymbatic course of fluorescence decay times of two (fast and medium) components in the temperature range from –60 to +10°C was observed. The third (slow) component showed only slight temperature dependence. The antisymbatic behavior of fluorescence lifetimes of the fast and medium components was explained on the assumption that some of the excited tryptophan molecules are transferred from a short-wave-length B-form with short fluorescence lifetime to a long-wavelength R-form with an intermediate fluorescence lifetime. This transfer occurred in the indicated temperature range.
Tài liệu tham khảo
Frauenfelder, H., and McMahon, B. (1998) Dynamics and function of proteins: the search for general concepts, Proc. Natl. Acad. Sci. USA, 95, 4795–4797.
Fitter, J., Lechner, R. E., Buldt, G., and Dencher, N. A. (1996) Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic inco-herent neutron scattering using oriented purple mem-branes, Proc. Natl. Acad. Sci. USA, 93, 7600–7605.
Frauenfelder, H., Sligar, S. G., and Wolynes, P. G. (1991) The energy landscapes and motions of proteins, Science, 254, 1598–1603.
Jackson, T. A., Lim, M., and Anfinrud, P. A. (1994) Complex nonexponential relaxation in myoglobin after photodissociation of MbCO: measurement and analysis from 2 ps to 56 μs, Chem. Phys., 180, 131–140.
Johnson, J. B., Lamb, D. C., Frauenfelder, H., Muller, J. D., McMahon, B., Nienhaus, G. U., and Young, R. D. (1996) Ligand binding to heme proteins, Biophys. J., 71, 1563–1573.
Paciarony, A., Cinelli, S., and Onori, G. (2002) Effect of the environment on the protein dynamical transition: a neutron scattering study, Biophys. J., 83, 1157–1164.
Palazzo, G., Mallardi, A., Hochkoeppler, A., Cordone, L., and Venturoli, G. (2002) Electron transfer kinetics in pho-tosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substates at room temperature, Biophys. J., 82, 558–568.
Kriegl, J. M., Forster, F. K., and Nienhaus, G. U. (2003) Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix, Biophys. J., 85, 1851–1870.
Mei, G., Di Venere, A., Agro, A. F., De Matteis, F., and Rosato, N. (2003) Dipolar relaxation times of tryptophan and tyrosine in glycerol and in proteins: a direct evaluation from their fluorescence decays, J. Fluoresc., 13, 467–477.
Malferrari, M., Savitsky, A., Mamedov, M. D., Milanovsky, G. E., Lubitz, W., Mobius, K., Semenov, A. Yu., and Venturoli, G. (2016) Trehalose matrix effects on charge-recombination kinetics in photosystem I of oxygenic photosynthesis at different dehydration levels, Biochim. Biophys. Acta, 1857, 1440–1454.
Schlamadinger, D. E., Gable, J. E., and Kim, J. E. (2009) Hydrogen bonding and solvent polarity markers in the UV resonance Raman spectrum of tryptophan: application to membrane proteins, J. Phys. Chem. B, 113, 14769–14778.
Dashnau, J. L., Zelent, B., and Vanderkooi, J. M. (2005) Tryptophan interactions with glycerol/water and tre-halose/sucrose cryosolvents: infrared and fluorescence spectroscopy and ab initio calculations, Biophys. Chem., 114, 71–83.
Chen, Y., and Barkley, M. D. (1998) Toward understanding tryptophan fluorescence in proteins, Biochemistry, 3, 9976–9982.
Burshtein, E. A. (1983) Intrinsic protein luminescence as a tool for studying fast structural dynamics, Mol. Biol. (Moscow), 17, 455–467.
Knox, P. P., Korvatovsky, B. N., Krasilnikov, P. M., Pashchenko, V. Z., Seifullina, N. Kh., Grishanova, N. P., and Rubin, A. B. (2016) Temperature dependence of protein fluorescence in Rb. sphaeroides reaction centers frozen to 80K in the dark or on the actinic light as the indicator of protein conformational dynamics, Dokl. Biochem. Biophys., 467, 105–109.
Knox, P. P., Lukashev, E. P., Korvatovskii, B. N., Gorokhov, V. V., Pashchenko, V. Z., Seifullina, N. Kh., Grishanova, N. P., and Rubin, A. B. (2016) A comparison of the temperature dependence of charge recombination in the ionradical pair P870+QA– and tryptophan fluorescence in the photosynthetic reaction centers of Rhodobacter sphaeroides, Biophysics, 61, 923–930.
Ross, J. A., and Jameson, D. M. (2008) Time-resolved methods in biophysics. 8. Frequency domain fluorometry: applications to intrinsic protein fluorescence, Photochem. Photobiol. Sci., 7, 1301–1312.
Olsson, C., Jansson, H., and Swenson, J. (2016) The role of trehalose for the stabilization of proteins, J. Phys. Chem. B, 120, 4723–4731.
Adams, P. D., Chen, Y., Ma, K., Zagorski, M. G., Sonnichsen, F. D., McLaughlin, M. L., and Barkley, M. D. (2002) Intramolecular quenching of tryptophan fluores-cence by the peptide bond in cyclic hexapeptides, J. Am. Chem. Soc., 124, 9278–9286.
Hayward, B. J., and Henry, B. B. (1976) Experimental manifestations of the local mode description of high energy polyatomic overtone spectra, Chem. Phys., 12, 387–396.
Tarasevich, B. N. (2012) IR-Spectra of Major Classes of Organic Compounds. Reference Materials [in Russian], MSU, Moscow.
Medvedev, E. S., and Osherov, V. I. (1983) Theory of Non-radiative Transitions in Multiatom Molecules [in Russian], Nauka, Moscow.
Emanuel, N. M., and Kuzmin, M. G. (1985) Experimental Techniques in Chemical Kinetics [in Russian], MSU, Moscow.
