Alkaline conformational transitions of ferricytochrome c studied by resonance Raman spectroscopy

Journal of the American Chemical Society

Volumn 120, Issue 44, 1998, Pages 11246-11255

  Döpner, Susanne ^a,b   Hildebrandt, Peter ^a   Resell, Federico I ^b   Mauk, A Grant ^b  

^a MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; FUNGAL PROTEIN;

ARTICLE; CHEMICAL REACTION; ELECTRON TRANSPORT; NONHUMAN; PH; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; YEAST;

EID: 0032508940     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9717572     Document Type: Article

References (54)

1. (a) Moore, G. R.; Pettigrew, G. W. Cytochromes c. Evolutionary, Structural and Physicochemical Aspects; Springer-Verlag: Berlin, 1990; pp 190-196.
2. (b) Wilson, M. T.; Greenwood, C. In Cytochrome c: A Multidisciplinary Approach; Scott, R. A., Mauk, A. G., Eds.; University Science Books: Mill Valley, CA, 1996; pp 611-634.
3. Theorell, H.; Åkesson, Å. J. Am. Chem. Soc. 1941, 63, 1804-1811.
4. Examples of proteins reported to exhibit pH-linked conformational states include reduced plastocyanin (Guss, J. M.; Harrowell, P. R.; Murata, M.; Norris, V. A.; Freeman, H. C. J. Mol. Biol. 1986, 192, 361-387), growth hormone (Holzman, T. F.; Dougherty, J. J.; Brems, D. N.; MacKenzie, N. E. Biochemistry 1990, 29, 1255-1261), the N-terminal lobe of transferrin (Dewan, J. C.; Mikami, B.; Hirose, M.; Sacchettini, J. C. Biochemistry 1993, 32, 11963-11968. Chahine, J. M. E. H.; Pakdaman, R. Eur. J. Biochem. 1995, 230, 1102-1110), and influenza virus hemagglutinin (Tatulian, S. A.; Tamm, L. K. J. Mol. Biol. 1996, 260, 312-316).
5. Examples of proteins reported to exhibit pH-linked conformational states include reduced plastocyanin (Guss, J. M.; Harrowell, P. R.; Murata, M.; Norris, V. A.; Freeman, H. C. J. Mol. Biol. 1986, 192, 361-387), growth hormone (Holzman, T. F.; Dougherty, J. J.; Brems, D. N.; MacKenzie, N. E. Biochemistry 1990, 29, 1255-1261), the N-terminal lobe of transferrin (Dewan, J. C.; Mikami, B.; Hirose, M.; Sacchettini, J. C. Biochemistry 1993, 32, 11963-11968. Chahine, J. M. E. H.; Pakdaman, R. Eur. J. Biochem. 1995, 230, 1102-1110), and influenza virus hemagglutinin (Tatulian, S. A.; Tamm, L. K. J. Mol. Biol. 1996, 260, 312-316).
6. Examples of proteins reported to exhibit pH-linked conformational states include reduced plastocyanin (Guss, J. M.; Harrowell, P. R.; Murata, M.; Norris, V. A.; Freeman, H. C. J. Mol. Biol. 1986, 192, 361-387), growth hormone (Holzman, T. F.; Dougherty, J. J.; Brems, D. N.; MacKenzie, N. E. Biochemistry 1990, 29, 1255-1261), the N-terminal lobe of transferrin (Dewan, J. C.; Mikami, B.; Hirose, M.; Sacchettini, J. C. Biochemistry 1993, 32, 11963-11968. Chahine, J. M. E. H.; Pakdaman, R. Eur. J. Biochem. 1995, 230, 1102-1110), and influenza virus hemagglutinin (Tatulian, S. A.; Tamm, L. K. J. Mol. Biol. 1996, 260, 312-316).
7. Examples of proteins reported to exhibit pH-linked conformational states include reduced plastocyanin (Guss, J. M.; Harrowell, P. R.; Murata, M.; Norris, V. A.; Freeman, H. C. J. Mol. Biol. 1986, 192, 361-387), growth hormone (Holzman, T. F.; Dougherty, J. J.; Brems, D. N.; MacKenzie, N. E. Biochemistry 1990, 29, 1255-1261), the N-terminal lobe of transferrin (Dewan, J. C.; Mikami, B.; Hirose, M.; Sacchettini, J. C. Biochemistry 1993, 32, 11963-11968. Chahine, J. M. E. H.; Pakdaman, R. Eur. J. Biochem. 1995, 230, 1102-1110), and influenza virus hemagglutinin (Tatulian, S. A.; Tamm, L. K. J. Mol. Biol. 1996, 260, 312-316).
8. Examples of proteins reported to exhibit pH-linked conformational states include reduced plastocyanin (Guss, J. M.; Harrowell, P. R.; Murata, M.; Norris, V. A.; Freeman, H. C. J. Mol. Biol. 1986, 192, 361-387), growth hormone (Holzman, T. F.; Dougherty, J. J.; Brems, D. N.; MacKenzie, N. E. Biochemistry 1990, 29, 1255-1261), the N-terminal lobe of transferrin (Dewan, J. C.; Mikami, B.; Hirose, M.; Sacchettini, J. C. Biochemistry 1993, 32, 11963-11968. Chahine, J. M. E. H.; Pakdaman, R. Eur. J. Biochem. 1995, 230, 1102-1110), and influenza virus hemagglutinin (Tatulian, S. A.; Tamm, L. K. J. Mol. Biol. 1996, 260, 312-316).
9. (a) Takano, T.; Dickerson, R. E. J. Mol. Biol. 1981, 153, 79-94.
10. (b) Takano, T.; Dickerson, R. E. J. Mol. Biol. 1981, 153, 95-115.
11. (c) Louie, G. V.; Hutcheon, W. L. B.; Brayer, G. D. J. Mol. Biol. 1988, 214, 527-555.
12. (d) Bushnell, G. W.; Louie, G. V.; Brayer, G. D. J. Mol. Biol. 1990, 214, 585-595.
13. (e) Berghuis, A. M.; Brayer, G. D. J. Mol. Biol. 1992, 223, 959-976.
14. Barker, P. D.; Mauk, A. G. J. Am. Chem. Soc. 1992, 114, 3619-3624.
15. Jordan, T.; Eads, J. C.; Spiro, T. G. Protein Sci. 1995, 4, 716-728 and references therein.
16. Weber, C.; Michel, B.; Bosshard, H. R. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 6687-6691.
17. (a) Spiro, T. G., Ed. Biological Applications of Roman Spectroscopy; Wiley New York, 1988; Vol. III.
18. (b) Spiro, T. G. In Iron Porphyrins, part two; Lever, A. B. P., Gray, H. B., Eds.; Addison-Wesley: London, 1983; pp 89-159.
19. (c) Kitagawa, T.; Ozaki, Y. Struct. Bonding 1987, 64, 71-114.
20. (a) Ferrer, J. C.; Guillemette, J. G.; Bogumil, R.; Inglis, S. C.; Smith, M.; Mauk, A. G. J. Am. Chem. Soc. 1993, 115, 7507-7508.
21. (b) Rosell, F. I.; Ferrer, J. C.; Mauk, A. G. J. Am. Chem. Soc. 1998, 120, 11234-11245.
22. (a) Cutler, R. L.; Pielak, G. J.; Mauk, A. G.; Smith, M. Protein Eng. 1987, 1, 95-99.
23. (b) Rafferty, S. P.; Pearce, L. L.; Barker, P. D.; Guillemette, J. G.; Kay, C. M.; Smith, M.; Mauk, A. G. Biochemistry 1990, 29, 9365-9369.
24. 10a
25. (a) Hildebrandt, P.; Heimburg, T.; Marsh, D.; Powell, G. L. Biochemistry 1990, 29, 1661-1668.
26. (b) Heibel, G. E.; Hildebrandt, P.; Ludwig, B.; Steinrücke, P.; Soulimane, T.; Buse, G. Biochemistry 1993, 32, 10866-10877.
27. Hildebrandt, P.; Vanhecke, F.; Buse, G.; Soulimane, T.; Mauk, A. G. Biochemistry 1993, 32, 10912-10922.
28. Döpner, S.; Hildebrandt, P.; Mauk, A. G.; Lenk, H.; Stempfle, W. Spectrochim. Acta 1996, 52A, 573-584.
29. Parthasarathi, N.; Hansen, C.; Yamaguchi, S.; Spiro, T. G. J. Am. Chem. Soc. 1987, 109, 3865-3871.
30. (a) Prendergast, K.; Spiro, T. G. J. Am. Chem. Soc. 1992, 114, 3793-3801.
31. (b) Sparks, L. D.; Anderson, K. K.; Medforth, C. J.; Smith, K. M.; Shelnutt, J. A. Inorg. Chem. 1994, 33, 2297-2302.
32. Hu, S.; Morris, I. K.; Singh, J. P.; Smith, K. M.; Spiro, T. G. J. Am. Chem. Soc. 1993, 115, 12446-12458.
33. Pearce, L. L.; Gärtner, A. L.; Smith, M.; Mauk, A. G. Biochemistry 1989, 28, 3152-3156.
34. (a) Wallace, C. J. A.; Mascagni, P.; Chait, B. T.; Collawn, J. F.; Paterson, Y.; Proudfoot, A. E. I.; Kent, S. B. H. J. Biol. Chem. 1989, 264, 15199-15209.
35. (b) Luntz, T. L.; Schejter, A.; Garber, E. A. E.; Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 3524-3528.
36. Frauenhoff, M. A.; Scott, R. A. Proteins 1992, 14, 202-212.
37. Berghuis, A. M.; Guillemette, J. G.; Smith, M.; Brayer, G. D. J. Mol. Biol. 1994, 235, 1326-1341.
38. Hildebrandt, P.; Vanhecke, F.; Heibel, G.; Mauk, A. G. Biochemistry 1993, 32, 14158-14164.
39. Cartling, B. Biophys. J. 1983, 43, 191-205.
40. Mitchell, M. L.; Li, X.-Y.; Kincaid, J. R.; Spiro, T. G. J. Phys. Chem. 1987, 97, 4690-4696.
41. The substitution of Thr78 by Ala evidently stabilizes Lys coordination to the heme iron so that the states IVa and IVb prevail even at neutral pH and their transitions to the states Va and Vb occur at higher pH than in the wild-type protein.
42. (a) Rodgers, K. R.; Reed, R. A.; Spiro, T. G. New J. Chem. 1992, 16, 533-535.
43. (b) Feis, A.; Marzocchi, M. P.; Paoli, M.; Smulevich, G. Biochemistry 1994, 33, 4577-4583.
44. 11a,12,17 we have denoted this conformational state as state II, which, however, is in conflict with the widely accepted nomenclature for the pH-dependent conformers of cytochrome c (cf. ref 2).
45. (a) Hildebrandt, P. Biochim. Biophys. Acta 1990, 1040, 175-186.
46. (b) Chottard, G.; Michelon, M.; Hervé, M.; Hervé, G. Biochim. Biophys. Acta 1987, 916, 402-410.
47. (a) Smith, H. T.; Staudenmayer, N.; Millet, F. Biochemistry 1977, 16, 4971-4974.
48. (b) Speck, S. H.; Ferguson-Miller, S.; Osheroff, N.; Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 55-59.
49. (c) Rieder, R.; Bosshard, H. R. J. Biol. Chem. 1980, 255, 4732-4739.
50. Banci, L.; Bertini, L.; Bren, K. L.; Gray, H. B.; Turano, P. Chem. Biol. 1995, 2, 377-383.
51. Davis, L. A.; Schejter, A.; Hess, G. P. J. Biol. Chem. 1974, 249, 2624-2632.
52. Smith, H. T.; Millet, F. Biochemistry 1980, 19, 1117-1120.
53. Tonge, P.; Moore, G. R.; Wharton, C. W. Biochem. J. 1989, 258, 599-605.
54. Bosshard, H. R. J. Mol. Biol. 1981, 153, 1125-1149.