Fluorescence of the Single Tryptophan of Cutinase: Temperature and pH Effect on Protein Conformation and Dynamics

Photochemistry and Photobiology

Volumn 78, Issue 1, 2003, Pages 15-22

  Martinho, J M G ^a   Santos, A M ^a   Fedorov, A ^a   Baptista, R P ^a   Taipa, M A ^a   Cabral, J M S ^a  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

CUTINASE; TRYPTOPHAN;

ANISOTROPY; ARTICLE; COMPLEX FORMATION; DYNAMICS; FLUORESCENCE; FUSARIUM SOLANI; HYDROGEN BOND; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; TEMPERATURE DEPENDENCE; ULTRAVIOLET IRRADIATION;

ANIMALS; CARBOXYLIC ESTER HYDROLASES; FLUORESCENCE; FLUORESCENCE POLARIZATION; FUSARIUM; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TRYPTOPHAN; ULTRAVIOLET RAYS;

FUSARIUM; FUSARIUM SOLANI;

EID: 0242365531     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2003)078<0015:FOTSTO>2.0.CO;2     Document Type: Article

References (46)

1. Kolattukudy, P. E. (1984) Cutinase from fungi and pollen. In Lipases (Edited by B. Borgström and T. Brockman), pp. 471-504. Elsevier, Amsterdam.
2. Martinez, C., P. de Geus, M. Lauwereys, G. Matthyssens and C. Cambillau (1992) Fusarium solani cutinase is a lipolytic enzime with a catalytic serine accessible to solvent. Nature 356, 615-618.
3. Longhi, S., M. Czjzek, V. Lamzin, A. Nicolas and C. Cambillau (1997) Atomic resolution (1.0Å) crystal structure of fusarium solani cutinase: stereochemical analysis. J. Mol. Biol. 268, 779-799.
4. Martinez, C., A. Nicolas, H. van Tilbeurgh, M.-P. Egloff, C. Cudrey, R. Verger and C. Cambillau (1994) Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33, 83-89.
5. Prompers, J. J., A. Groeoewegen, C. W. Hilbers and H. A. M. Pepermans (1999) Backbone dynamics of fusarium solani pisi cutinase probed by nuclear magnetic resonance: the lack of interfacial activation revisited. Biochemistry 38, 5315-5327.
6. Weisenborn, P. C. M., H. Meder, M. R. Egmond, T. J. W. G. Visser and A. van Hoek (1996) Photophysics of the single tryptophan residue in fusarium solani cutinase: evidence for the occurrence of conformational substates with unusual fluorescence behaviour. Biophys. Chem. 58, 281-288.
7. Prompers, J. J., C. W. Hilbers and H. A. M. Pepermans (1999) Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of fusarium solani pisi cutinase. FEBS Lett. 456, 409-416.
8. Vanhooren, A., B. Devreese, K. Vanhee, J. Van Beeumen and I. Hanssens (2002) Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin. Biochemistry 41, 11035-11043.
9. Petersen, M. T. N., Z. Gryczynski, J. Lakowicz, P. Fojan, S. Pedersen, E. Petersen and S. B. Petersen (2002) High probability of disrupting a disulphide bridge mediated by an endogeneous excited tryptophan residue. Protein Sci. 11, 588-600.
10. Ichiye, T. and M. Karplus (1983) Fluorescence depolarization of tryptophan residues in proteins: a molecular dynamics study. Biochemistry 22, 2884-2893.
11. Gallay, J., J. Sopková and M. Vincent (2000) The conformation flexibility of domain III of Annexin V is modulated by calcium, pH and binding to membrane/water interfaces. In Topics in Fluorescence Spectroscopy, Vol. VI (Edited by J. R. Lakowicz), pp. 123-173. Kluwer Academic/Plenum Publishers, New York.
12. Carvalho, C. M. L., M. R. Aires-Barros and J. M. S. Cabral (1999) Cutinase: from molecular level to bioprocess development. Biotechnol. Bioeng. 66, 17-34.
13. Farinha, J. P. S., S. Piçarra, K. Miesel and J. M. G. Martinho (2001) Fluorescence study of the coil-globule transition of a PEO chain in toluene. J. Phys. Chem. B 105, 10536-10545.
14. Marquardt, D. W. (1963) An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11, 431.
15. Burstein, E. A., N. S. Vedenkina and M. N. Ivkova (1973) Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18, 263-279.
16. Eftink, M. R. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482-501.
17. Melo, E. P., S. M. B. Costa and J. M. S. Cabral (1996) Denaturation of a recombinant cutinase from fusarium solani in AOT-iso-octane reverse micelles: a steady-state fluorescence study. Photochem. Photobiol. 63, 169-175.
18. Lakowicz, J. R. (2000) On spectral relaxation in proteins. Photochem. Photobiol. 72, 421-437.
19. Szabo, A. G. and D. M. Rayner (1980) Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102, 554-563.
20. Petrich, J. W., M. C. Chang, D. B. McDonald and G. R. Fleming (1983) On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105, 3824-3832.
21. Chen, Y., B. Liu, H.-T. Yu and M. D. Barkley (1996) The peptide bond quenches indole fluorescence. J. Am. Chem. Soc. 118, 9271-9278.
22. Chen, Y. and M. D. Barkley (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982.
23. Hudson, B. S. (1999) An ionization/recombination mechanism for complexity of the fluorescence of tryptophan in proteins. Acc. Chem. Res. 32, 297-300.
24. Hudson, B. S., J. M. Huston and G. Soto-Campos (1999) A reversible "dark state" mechanism for complexity of the fluorescence of tryptophan in proteins. J. Phys. Chem. A 103, 2227-2234.
25. Callis, P. R. and B. K. Burgess (1997) Tryptophan fluorescence shifts in proteins from hybrid simulations: an electrostatic approach. J. Phys. Chem. B 101, 9429-9432.
26. Pal, S. K., J. Peon and A. H. Zewail (2002) Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution. Proc. Natl. Acad. Sci. USA 99, 1763-1768.
27. Toptygin, D. and L. Brand (2000) Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: a quantitative model. Chem. Phys. Lett. 322, 496-502.
28. Toptygin, D., R. S. Savtchenko, N. D. Meadow and L. Brand (2001) Homogeneous spectrally- and time-resolved fluorescence emission from single-tryptophan mutants of IIAGlc protein. J. Phys. Chem. B 105, 2043-2055.
29. Lakowicz, J. R. and H. Cherek (1980) Dipolar relaxation in proteins on the nanosecond timescale observed by wavelength-resolved phase fluorometry of tryptophan fluorescence. J. Biol. Chem. 255, 831-834.
30. Silva, N. D. and F. G. Prendergast (1996) Tryptophan dynamics of the FK506 binding protein: time-resolved fluorescence and simulations. Biophys J. 70, 1122-1137.
31. Nanda, V. and L. Brand (2000) Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan. Proteins: Struct. Funct. Genet. 40, 112-125.
32. Nanda, V., S.-M. Liang and L. Brand (2000) Hydrophobic clustering in acid-denatured IL-2 and fluorescence of a Trp NH‴π H-bond. Biophys. Biochem. Res. Commun. 279, 770-778.
33. Herbich, J., M. Kijak, A. Zielinska, R. P. Thummel and J. Waluk (2002) Fluorescence quenching by pyridine and derivatives induced by intermolecular hydrogen bonding to pyrrole-containing heteroaromatics. J. Phys. Chem. A 106, 2158-2163.
34. Yatsuhashi, T. and H. Inoue (1997) Molecular mechanism of radiationless deactivation of aminoanthraquinones through intermolecular hydrogen-bonding interaction with alcohols and hydroperoxides. J. Phys. Chem. A. 101, 8166-8173.
35. Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2nd ed., Kluwer Academic/Plenum Publishers, New York.
36. Grossweiner, L. I. and Y. Usui (1970) The role of the hydrated electron in photoreduction of cystine in the presence of indole. Photochem. Photobiol. 11, 53-56.
37. Grossweiner, L. I. and Y. Usui (1971) Flash photolysis and inactivation of aqueous lysozyme. Photochem. Photobiol. 13, 195-214.
38. Shen, X. and J. R. Knutson (2001) Subpicosecond fluorescence spectra of tryptophan in water. J. Phys. Chem. B 105, 6260-6265.
39. Valeur, B. and G. Weber (1977) Resolution of the fluorescence excitation spectrum of indole into the 1La and 1Lb excitation bands. Photochem. Photobiol. 25, 441-444.
40. Yamamoto, Y. and J. Tanaka (1972) Polarized absorption-spectra of crystals of indole and its related compounds. Bull. Chem. Soc. Jpn. 45, 1362.
41. Callis, P. R. (1997) 1La and 1Lb transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278, 113-150.
42. Lipari, G. and A. Szabo (1980) Effect of vibrational motion on fluorescence depolarization and nuclear magnetic-resonance relaxation in macromolecules and membranes. Biophys. J. 30, 489-506.
43. Levy, R. M. and A. Szabo (1982) Initial fluorescence depolarization of tyrosines in proteins. J. Am. Chem. Soc. 104, 2073-2075.
44. Kinosita, K. J., S. Kawato and A. Ikegami (1977) Theory of fluorescence polarization decay in membranes. Biophys. J. 20, 289-305.
45. Tcherkasskaya, O., O. B. Ptitsyn and J. R. Knutson (2000) Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry 39, 1879-1889.
46. Semisotnov, G. V., K. K. Zikherman, S. B. Kasatkin, O. B. Ptitsyn and E. V. Anufrieva (1981) Polarized luminescence and mobility of tryptophan residues in polypeptide chains. Biopolymers 20, 2287-2309.