Ionization potentials of fluoroindoles and the origin of nonexponential tryptophan fluorescence decay in proteins

Journal of the American Chemical Society

Volumn 127, Issue 11, 2005, Pages 4104-4113

  Liu, Tiqing ^a   Callis, Patrik R ^a   Hesp, Ben H ^b   De Groot, Mattijs ^c   Buma, Wybren Jan ^c   Broos, Jaap ^b  

^a MONTANA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONS; FLUORESCENCE; IONIZATION; QUENCHING;

ELECTRON TRANSFER QUENCHING; FLUORESCENCE DACAY; FLUOROINDOLES; MUTANTS;

PROTEINS;

1 METHYLINDOLE; 2 FLUORO 3 METHYLINDOLE; 2 FLUOROINDOLE; 3 FLUOROINDOLE; 4 FLUORO 3 METHYLINDOLE; 4 FLUOROINDOLE; 5 FLUORO 3 METHYLINDOLE; 5 FLUOROINDOLE; 5 FLUOROTRYPTOPHAN; 5 HYDROXY 3 METHYLINDOLE; 5 METHYLINDOLE; 6 FLUORO 3 METHYLINDOLE; 6 FLUOROINDOLE; 7 AZA 3 METHYLINDOLE; 7 FLUORO 3 METHYLINDOLE; 7 FLUOROINDOLE; BENZENE; FLUOROBENZENE; FLUOROINDOLE DERIVATIVE; INDOLE DERIVATIVE; MUTANT PROTEIN; SKATOLE; TOLUENE; TRYPTOPHAN; UNCLASSIFIED DRUG;

AB INITIO CALCULATION; ARTICLE; CHEMICAL STRUCTURE; DIPOLE; ELECTRON TRANSPORT; EXCITATION; FLUORESCENCE; IONIZATION; NONPHOTOCHEMICAL QUENCHING; PROTEIN BINDING; QUANTUM MECHANICS; SUBSTITUTION REACTION;

ELECTROCHEMISTRY; FLUORESCENCE POLARIZATION; INDOLES; PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN;

EID: 15744370492     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja043154d     Document Type: Article

References (78)

1. Beechem, J. M.; Brand, L. Annu. Rev. Biochem. 1985, 54, 43-71.
2. Eftink, M. R. Methods Biochem. Anal. 1991, 35, 127-205.
3. Lakowicz, J. Principles of Fluorescence Spectroscopy, 2nd ed.; Plenum: 1999.
4. Smirnov, A. V.; English, D. S.; Rich, R. L.; Lane, J.; Teyton, L.; Schwabacher, A. W.; Luo, S.; Thornburg, R. W.; Petrich, J. W. J. Phys. Chem. B 1997, 101 (15), 2758-2769.
5. Prendergast, F. G. Curr. Opin. Struct. Biol. 1991, 1, 1054-1059.
6. Privat, J.-P.; Wahl, P.; Auchet, J.-C. Biophys. Chem. 1979, 9, 223-233.
7. Petrich, J. W.; Chang, M. C.; McDonald, D. B.; Fleming, G. R. J. Am. Chem. Soc. 1983, 105, 3824-3832.
8. Dahms, T. E. S.; Willis, K. J.; Szabo, A. G. J. Am. Chem. Soc. 1995, 117, 2321-2326.
9. Hellings, M.; DeMaeyer, M.; Verheyden, S.; Hao, Q.; VanDamme, E. J. M.; Peumans, W. J.; Engelborghs, Y. Biophys. J. 2003, 85, 1894-1902.
10. Ross, J. B. A.; Wyssbrod, H. R.; Porter, R. A.; Schwartz, G. P.; Michaels, C. A.; Laws, W. R. Biochemistry 1992, 31 (6), 1585-1594.
11. Lakowicz, J. Photochem. Photobiol. 2000, 72, 421-437.
12. Bajzer, Z.; Prendergast, F. G. Biophys. J. 1993, 65, 2313-2323.
13. Hudson, B. S.; Huston, J. M.; Soto-Campos, G. J. Phys. Chem. A 1999, 103, 2227-2234.
14. Wlodarczyk, J.; Kierdaszuk, B. Biophys. J. 2003, 85 (1), 589-598.
15. De-Beuckeleer, K.; Volckaert, G.; Engelborghs, Y. Proteins 1999, 36, 42-53.
16. Weisenborn, P. C. M.; Meder, H.; Egmond, M. R.; Visser, T. J. W. G.; van Hoek, A. Biophys. Chem. 1996, 58, 281-288.
17. Cowgill, R. W. Arch. Biochem. Biophys. 1963, 100, 36-44.
18. Petrich, J. W.; Chang, M. C.; Fleming, G. R. NATO ASl Ser. 1985, 85, 77-80.
19. Ricci, R. W.; Nesta, J. M. J. Phys. Chem. 1976, 80, 974-980.
20. Chen, Y.; Liu, B.; Yu, H.-T.; Barkley, M. D. J. Am. Chem. Soc. 1996, 118, 9271-9278.
21. Chen, Y.; Barkley, M. D. Biochemistry 1998, 37, 9976-9982.
22. Ababou, A.; Bombarda, E. Protein Sci. 2001, 10, 2102-2113.
23. Callis, P. R.; Vivian, J. T. Chem. Phys. Lett. 2003, 369, 409-414.
24. Callis, P. R.; Liu, T. J. Phys. Chem. B 2004, 108, 4248-4259.
25. Broos, J.; Maddalena, F.; Hesp, B. H. J. Am. Chem. Soc. 2004, 126, 22-23.
26. Dijkstra, D. S.; Broos, J.; Visser, A. J. W. G.; vanHoek, A.; Robillard, G. T. Biochemistry 1997, 36 (16), 4860-4866.
27. 3M1 and NATA are useful model compounds. NATA has two amides connected to the indole ring just as in the protein and does not have the ammonium and carboxylate characteristic of the free amino acid Trp at pH 7. The amides are separated from the system of the indole ring by two saturated carbons. Therefore, 3M1 has very nearly the same electronic properties, without the possibility of electron transfer to the amides.
28. Rehm, D.; Weller, A. Isr. J. Chem. 1970, 8, 259-271.
29. Dijkstra, D. S.; Broos, J.; Robillard, G. T. Anal. Biochem. 1996, 240 (1), 142-147.
30. Broos, J.; Gabellieri, E.; Biemans-Oldehinkel, E.; Strambini, G. B. Protein Sci. 2003, 12 (9), 1991-2000.
31. Holst, P. B.; Anthoni, U.; Christophersen, C.; Larsen, S.; Nielsen, P. H.; Puschl, A. Adv. Chem. Phys. 1998, 52 (6), 683-693.
32. Mor, M.; Rivara, S.; Silva, C.; Bordi, F.; Plazzi, P. V.; Spadoni, G.; Diamantini, G.; Balsamini, C.; Tarzia, G.; Fraschini, F.; Lucini, V.; Nonno, R.; Stankov, B. M. J. Med. Chem. 1998, 41 (20), 3831-3844.
33. Wayland, E.; Noland, C. R. J. Org. Chem. 1967, 32, 828-832.
34. Gaussian 98, revision A.11.3; Gaussian, Inc.: Pittsburgh, PA, 2002.
35. Lee, C.; Yang, W.; Parr, R. G. Phys. Rev. B 1988, 37, 785.
36. Wetmore, S. D.; Boyd, R. J.; Eriksson, L. A. Chem. Phys. Lett. 2000, 322, 129-135.
37. MOLCAS5.4, version 5.4; Lund University: Sweden, 2000.
38. Pierloot, K.; Dumez, B.; Widmark, P.-O.; Roos, B. O. Theor. Chim. Acta 1995, 90, 87.
39. Ridley, J.; Zemer, M. Theor. Chim. Acta (Berl.) 1973, 32, 111.
40. Nishimoto, K.; Malaga, N. Z. Phys. Chem. (Frankfurt) 1957, 13, 140.
41. Li, J.; Williams, B.; Cramer, C. J.; Truhlar, D. G. J. Phys. Chem. 1999, 110, 724-733.
42. Callis, P. R. Int. J. Quantum. Chem. 1984, S18, 579-588.
43. Rijkenberg, R. A.; Buma, W. J.; van Walree, C. A.; Jenneskens, L. W. J. Phys. Chem. A 2002, 106 (21), 5249-5262.
44. Rijs, A. M.; Backus, E. H. G.; de Lange, C. A.; Westwood, N. P. C.; Janssen, M. H. M. Electron Spectrosc. Relat. Phenom. 2000, 112, 151.
45. Nemeth, G. I.; Selzle, H. L.; Schlag, E. W. Chem. Phys. Lett. 1993, 215 (1-3), 151-155.
46. Fujisawa, S.; Ohno, K.; Masuda, S.; Harada, Y. J. Am. Chem. Soc. 1986, 108 (21), 6505-6511.
47. Lu, K. T.; Eiden, G. C.; Weisshaar, J. C. J. Phys. Chem. 1992, 96 (24), 9742-9748.
48. Hager, J. W.; Wallace, S. C. Anal. Chem. 1988, 60, 5-10.
49. Lin, L. L.; Zhang, S.; Tzeng, W. B. J. Chem. Phys. 2004, 120, 5057-5063.
50. Eftink, M. R.; Selvidge, L. A.; Callis, P. R.; Rehms, A. A. J. Phys. Chem. 1990, 94 (9), 3469-3479.
51. Valeur, B.; Weber, G. Photochem. Photobiol. 1977, 25, 441-444.
52. Callis, P. R. Methods Enzymol. 1997, 278, 113-150.
53. Shen, X. H.; Knutson, J. R. J. Phys. Chem. B 2001, 105 (26), 6260-6265.
54. Vivian, J. T.; Callis, P. R. Biophys. J. 2001, 80, 2093-2109.
55. Wong, C.-Y.; Eftink, M. R. Biochemistry 1998, 37, 8938-8946.
56. Ross, J. B. A.; Szabo, A. G.; Hogue, C. W. V. Methods Enzymol. 1997, 278, 151.
57. Das, K.; Ashby, K. D.; Smirnov, A. V.; Reinach, F. C.; Petrich, J. W.; Farah, C. S. Photochem. Photobiol. 1999, 70 (5), 719-730.
58. Wong, C.-Y.; Eftink, M. R. Protein Sci. 1997, 6, 689-697.
59. Toptygin, D.; Savtchenko, R. S.; Meadow, N. D.; Brand, L. J. Phys. Chem. B 2001, 105, 2043-2055.
60. Bixon, M.; Jortner, J. Adv. Chem. Phys. 1999, 106, 35-202.
61. Hopfield, J. J. Proc. Natl. Acad. Sci., U.S.A. 1974, 71, 3640-3644.
62. Levich, V. G.; Dogonadze, R. R. Dokl. Akad. Nauk SSSR, Ser. Fiz. Khim. 1959, 124, 123-126.
63. Kestner, N. R.; Logan, J.; Jortner, J. J. Phys. Chem. 1974, 78, 2148-2166.
64. Marcus, R. A.; Sutin, N. Biochim. Biophys. Acta 1985, 811, 265-322.
65. Barzykin, A. V.; Frantsuzov, P. A.; Seki, K.; Tachiya, M. Adv. Chem. Phys. 2002, 123, 511-616.
66. Weber, G.; Shinitzky, M. Proc. Natl. Acad. Sci. U.S.A. 1970, 65 (4), 823-830.
67. Zhang, L. Y.; Friesner, R. A.; Murphy, R. B. J. Chem. Phys. 1997, 107 (2), 450-459.
68. Blumen, A.; Manz, J. J. Chem. Phys. 1979, 71 (11), 4694-4702.
69. Klafter, J.; Shlesinger, M. F. Proc. Nat. Acad. Sci. U.S.A. 1986, 83 (4), 848-851.
70. Adams, P. D.; Chen, Y.; Ma, K.; Zagorski, M. G.; Sonnichsen, F. D.; McLaughlin, M. L.; Barkley, M. D. J. Am. Chem. Soc. 2002, 124, 9278-9286.
71. Yang, H.; Luo, G.; Karnchanaphanurach, P.; Louie, T.-M.; Rech, I.; Cova, S.; Xun, L.; Xie, X. S. Science 2003, 302, 262-266.
72. 67 further confounding attempts to correlate distance and lifetime.
73. For example, analysis of the decays of 5FTrp-containing proteins (Table 3) while fixing a second component indicate that a 50% shorter lifetime with a 10% amplitude will remain unnoticed.
74. Broos, J.; Pas, H. H.; Robillard, G. T. J. Am. Chem. Soc. 2002, 124 (24), 6812-6813.
75. Meech, S. R.; Lee, A.; Phillips, D. Chem. Phys. 1983, 80, 317-328.
76. Pal, S. K.; Peon, J.; Bagchi, B.; Zewail, A. H. J. Phys. Chem. B 2002, 106 (48), 12376-12395.
77. Chen, Y.; Gai, F.; Petrich, J. W. J. Phys. Chem. 1994, 98 (8), 2203-2209.
78. Newton, M. D. Theor. Chem. Acc. 2003, 110 (5), 307-321.