Identification of the predominant non-native histidine ligand in unfolded cytochrome c

Biochemistry

Volumn 36, Issue 41, 1997, Pages 12535-12541

  Colón, Wilfredo ^a,d   Wakem, L Paul ^b   Sherman, Fred ^b   Roder, Heinrich ^a,c  

^a FOX CHASE CANCER CENTER   (United States)

^b UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d RENSSELAER POLYTECHNIC INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CYTOCHROME C; GLUTAMINE; HEME; HISTIDINE; LIGAND; METHIONINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTEIN FOLDING;

ANIMALS; BINDING SITES; CYTOCHROME C GROUP; HISTIDINE; HORSES; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; PROTEIN BINDING; PROTEIN FOLDING;

EQUUS CABALLUS;

EID: 0030816577     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971697c     Document Type: Article

References (31)

1. Babul, J., and Stellwagen, E. (1971) Biopolymers 10, 2359-2361.
2. Babul, J., and Stellwagen, E. (1972) Biochemistry 11, 1195-1200.
3. Tsong, T. Y. (1975) Biochemistry 14, 1542-1547.
4. Muthukrishnan, K., and Nail, B. T. (1991) Biochemistry 30, 4706-4710.
5. Roder, H., Elöve, G. A., and Englander, S. W. (1988) Nature 335, 700-704.
6. Elöve, G. A., and Roder, H. (1991) ACS Symp. Ser. 470, 50-63.
7. Elöve, G. A., Bhuyan, A. K., and Roder, H. (1994) Biochemistry 33, 6925-6935.
8. Sosnick, T. R., Mayne, L., Hiller, R., and Englander, S. W. (1994) Nat. Struct. Biol. 1, 149-156.
9. Colon, W., Elöve, G. A., Wakem, L. P., Sherman, F., and Roder, H. (1996) Biochemistry 35, 5538-5549.
10. Yeh, S.-R., Takahashi, S., Fan, B., and Rousseau, D. L. (1997) Nat. Struct. Biol. 4, 51-56.
11. Pierce, M. M., and Nall, B. T. (1997) Protein Sci. 6, 618-627.
12. Sauder, J. M., MacKenzie, N. E., and Roder, H. (1996) Biochemistry 35, 16852-16862.
13. Hickey, D. R., Jayaraman, K., Goodhue, C. T., Shah, J., Fingar, S. A., Clements, J. M., Hosokawa, Y., Tsunasawa, S., and Sherman, F. (1991) Gene 105, 73-81.
14. Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987) Methods Enzymol. 154, 367-383.
15. Pace, C. N. (1986) Methods Enzymol. 131, 266-280.
16. Santoro, M. M., and Bolen, D. W. (1992) Biochemistry 31, 4901-4907.
17. Khorasanizadeh, S., Peters, I. D., Butt, T. R., and Roder, H. (1993) Biochemistry 32, 7054-7063.
18. Ikai, A., Fish, W. W., and Tanford, C. (1973) J. Mol. Biol. 73, 165-184.
19. Brems, D. N., and Stellwagen, E. (1983) J. Biol. Chem. 258, 3655-3660.
20. Takahashi, S., Yeh, S.-R., Das, T. K., Chan, C.-K., Gottfried, D. S., and Rousseau, D. L. (1997) Nat. Struct. Biol. 4, 44-50.
21. Moore, G. R., and Pettigrew, G. W. (1990) Cytochrome c: evolutionary, structural and physiochemical aspects, Springer-Verlag, Berlin.
22. Bushnell, G. W., Louie, G. V., and Brayer, G. D. (1990) J. Mol. Biol. 214, 585-595.
23. Qin, W., Sanishvili, R., Plotkin, B., Schejter, A., and Margoliash, E. (1995) Biochim. Biophys. Acta 1252, 87-94.
24. Sosnick, T. R., Mayne, L., and Englander, S. W. (1996) Proteins 24, 413-426.
25. Chan, C.-K., Hu, Y., Takahashi, S., Rousseau, D. L., Eaton, W. A., and Hofrichter, J. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 1779-1784.
26. Godbole, S., and Bowler, B. E. (1997) J. Mol. Biol. 268, 816-821.
27. Martinez, S., Huang, D., Szczepaniak, A., Cramer, W., and Smith, J. (1994) Structure 2, 95-105.
28. Gadsby, P. M. A., and Thomson, A. J. (1990) J. Am. Chem. Soc. 112, 5003-5011.
29. Cheesman, M. R., Greenwood, C., and Thomson, A. J. (1991) Adv. Inorg. Chem. 36, 201-255.
30. Hawkins, B. K., Hilgen-Willis, S., Pielak, G. J., and Dawson, J. H. (1994) J. Amer. Chem. Soc. 116, 3111-3112.
31. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.