Protein conformational dynamics probed by single-molecule electron transfer

Science

Volumn 302, Issue 5643, 2003, Pages 262-266

  Yang, Haw ^a,d   Luo, Guobin ^a   Karnchanaphanurach, Pallop ^a   Louie, Tai Man ^b   Rech, Ivan ^c   Cova, Sergio ^c   Xun, Luying ^b   Xie, X Sunney ^a  

^a HARVARD UNIVERSITY   (United States)

^b WASHINGTON STATE UNIVERSITY   (United States)

^c POLITECNICO DI MILANO   (Italy)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CONFORMATIONS; ELECTRON TRANSITIONS; FLUORESCENCE; MOLECULAR STRUCTURE; PHOTONS;

TIME SCALES;

PROTEINS;

FLAVINE NUCLEOTIDE; OXIDOREDUCTASE; TYROSINE;

ELECTRON; PROTEIN;

ARTICLE; CATALYSIS; CORRELATION ANALYSIS; ELECTRON TRANSPORT; FLUORESCENCE; FORCE; MOLECULAR DYNAMICS; MOLECULE; PHOTOCHEMISTRY; PHOTON; PRIORITY JOURNAL; PROTEIN CONFORMATION;

AMINO ACID SUBSTITUTION; CATALYSIS; CHEMISTRY, PHYSICAL; COMPUTER SIMULATION; ELECTRONS; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; FLAVINS; FLUORESCENCE; FMN REDUCTASE; HYDROGEN BONDING; LIKELIHOOD FUNCTIONS; MATHEMATICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOTONS; PROTEIN CONFORMATION; SERINE; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS; TYROSINE;

EID: 0141993702     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1086911     Document Type: Article

References (42)

1. S. M. Nie, R. N. Zare, Annu. Rev. Biophys. Biomol. Struct. 26, 567 (1997).
2. X. S. Xie, J. K. Trautman, Annu. Rev. Phys. Chem. 49, 441 (1998).
3. W. E. Moerner, M. Orrit, Science 283, 1670 (1999).
4. S. Weiss, Science 283, 1676 (1999).
5. H. P. Lu, L-Y. Xun, X. S. Xie, Science 282, 1877 (1998).
6. A. M. van Oijen et al., Science 301, 1235 (2003).
7. H. P. Lu, X. S. Xie, J. Phys. Chem. B 101, 2753 (1997).
8. X. W. Zhuang et al., Science 288, 2048 (2000).
9. H. Yang, X. S. Xie, J. Chem. Phys. 117, 10965 (2002).
10. M. Fontecave, R. Eliasson, P. Reichard, J. Biol. Chem. 262, 12325 (1987).
11. M. Engelman, S. Ramaswamy, V. Niviére, M. Fontecave, H. Eklund, Biochemistry 38, 7040 (1999).
12. P. A. W. van den Berg, A. J. W. G. Visser, in New Trends in Fluorescence Spectroscopy: Applications to Chemical and Life Sciences, B. Valeur, J.-C. Brochon, Eds. (Springer, New York, 2001), pp. 457-485.
13. Materials and methods are available as supporting material on Science Online.
14. N. Mataga et al., J. Phys. Chem. B 104, 10667 (2000).
15. D. Zhong, A. H. Zewail, Proc. Natl. Acad. Sci. U.S.A. 98, 11867 (2001).
16. T. Louie, H. Yang, P. Karnchanaphanurach, X. S. Xie, L.-Y. Xun, J. Biol. Chem. 277, 39450 (2002).
17. To verify that the surface tethering introduces no complications, we also immobilized the Fre/FAD complex in 1% agarose gel between two cover slips with the method described in (5). We observed the same lifetime fluctuation of single Fre/FAD complexes tethered on quartz surface as in the agarose gel, although the agarose gel introduced a weak fluorescence background.
18. S. Cova, A. Laciata, M. Ghioni, G. Ripamonti, T. A. Louis, Rev. Sci. Instrum. 60, 1104 (1989).
19. S. Cova, M. Ghioni, A. Lacaita, S. Samori, F. Zappa, Appl. Optics 35, 1956 (1996).
20. X. S. Xie, R. C. Dunn, Science 265, 361 (1994).
21. W. P. Ambrose, P. M. Goodwin, J. C. Martin, R. A. Keller, Science 265, 364 (1994).
22. L. Edman, U. Mets, R. Rigler, Proc. Natl. Acad. Sci. U.S.A. 93, 6710 (1996).
23. Y.-W. Jia et al., Proc. Natl. Acad Sci. U.S.A. 94, 7932 (1997).
24. C. Eggeling, J. R. Fries, L Brand, R. Günter, C. A. M. Seidel, Proc. Natl. Acad. Sci. U.S.A. 95, 1556 (1998).
25. M. Köllner, J. Wolfrum, Chem. Phys. Lett. 200, 199 (1992).
26. Y. Duan, P. A. Kollman, Science 282, 740 (1998).
27. R. A. Marcus, N. Sutin, Biochim. Biophys. Acta 811, 265 (1985).
28. J. Jortner, M. Bixon, Eds., Electron Transfer - From Isolated Molecules to Biomolecules (Wiley, New York, 1999), vol. 106.
29. M. Marchi, J. N. Gehlen, D. Chandler, M. Newton, J. Am. Chem. Soc. 115, 4178 (1993).
30. J. N. Gehlen, M. Marchi, D. Chandler, Science 263, 499 (1994).
31. C. C. Moser, J. M. Keske, K. Warncke, R. S. Farid, P. L. Dutton, Nature 355, 796 (1992).
32. H. B. Gray, J. R. Winkler, Annu. Rev. Biochem. 65, 537 (1996).
33. D. Kleinfeld, M. Y. Okamura, G. Feher, Biochemistry 23, 5780 (1984).
34. P. Siders, R. J. Cave, R. A. Marcus, J. Chem. Phys. 81, 5613 (1984).
35. J. A. Mccammon, P. G. Wolynes, M. Karplus, Biochemistry 18, 927 (1979).
36. J.-P. Bouchaud, A. Georges, Phys. Rep. Rev. Sec. Phys. Lett. 195, 12 (1990).
37. R. Metzler, J. Klafter, Phys. Rep. Rev. Sec. Phys. Lett. 339, 1 (2000).
38. R. Metzler, E. Barkai, J. Klafter, Phys. Rev. Lett. 82, 3563 (1999).
39. H. Frauenfelder, S. G. Sligar, P. G. Wolynes, Science 254, 1598 (1991).
40. C. A. Angell, Science 267, 1924 (1995).
41. T. A. Jackson, M. H. Lim, P. A. Anfinrud, Chem. Phys. 180, 131 (1994).
42. Supported by NIH (R01GM61577-01, single-molecule biophysics) and in part by the Natural and Accelerated Bioremediation Research project of the Offices of Sciences, U.S. Department of Energy (DE-FG02-00ER62891, flavin enzymology). We thank R. A. Marcus, Y. Klafter, M. Karplus, D. Reichman, M. Okamura, S. G. Boxer, and I. Andricioaei for helpful discussions and V. Niviére for providing the protein coordinates used in MD simulation (Fig. 1A).