Ligand perturbation effects on a pseudotetrahedral Co(II)(His)3-ligand site: A magnetic circular dichroism study of the Co(II)-substituted insulin hexamer

Journal of Biological Chemistry

Volumn 272, Issue 2, 1997, Pages 1088-1094

  Brader, Mark L ^d   Kaarsholm, Niels C ^b   Harnung, Sven E ^c   Dunn, Michael F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NOVO NORDISK A S   (Denmark)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

^d ELI LILLY AND COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CARBONATE DEHYDRATASE; COBALT; HISTIDINE; INSULIN; METAL ION; PHENOL DERIVATIVE; ZINC;

ARTICLE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; LIGAND BINDING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN STABILITY;

CIRCULAR DICHROISM; COBALT; HISTIDINE; INSULIN; MODELS, CHEMICAL; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ATOMIC;

EID: 0031021582     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.2.1088     Document Type: Article

References (46)

1. Bertini, I. (1986) in Zinc Enzymes, Progress in Inorganic Biochemistry and Biophysics (Bertini, I., Luchinat, C., Maret, W., and Zeppezauer, M., eds) Vol. 1, pp. 1-640, Birkhauser, Basel
2. Lippard, S. J., and Berg, J. M. (1994) Principles of Bioinorganic Chemistry, pp. 257-274, University Science Books, Mill Valley, CA
3. Brader, M. L., and Dunn, M. F. (1991) Trends Biochem. Sci. 16, 341-345
4. Derewenda, U., Derewenda, Z., Dodson, E. J., Dodson, G. G., Reynolds, C. D., Smith, G. D., Sparks, C., and Swenson, D. (1989) Nature 338, 594-596
5. Eriksson, A. E., Jones, T. A., and Liljas, A. (1988) Proteins Struct. Funct. Genet. 4, 274-282
6. Dideberg, O., Charlier, P., Dive, G., Joris, B., Frere, J. M., and Ghuysen, J. M. (1982) Nature 299, 469-470
7. Bode, W., Gomis-Ruth, F. X., Huber, R., Zwilling, R., and Stocker, W. (1992) Nature 358, 164-167
8. Sutton, B. J., Artymiuk, P. J., Cordero-Borboa, A. E., Little, C., Phillips, D. C., and Waley, S. G. (1987) Biochem. J. 248, 181-188
9. Stocker, W., and Bode, W. (1995) Curr. Opin. Struct. Biol. 5, 383-390
10. Bertini, I. (1983) in The Coordination Chemistry of Metalloenzymes (Bertini, I., Drago, R. S., and Luchinat, C., eds) pp. 1-18, D. Reidel Publishing Co., Dordrecht, Holland
11. Bicknell, R., Schaffer, A., Waley, S. G., and Auld, D. S. (1986) Biochemistry 25, 7208-7215
12. Shi, Y., Beger, R. D., and Berg, J. M. (1993) Biophys. J. 64, 749-753
13. Flamini, A., Sestili, L., and Furiani, C. (1971) Inorg. Chim. Acta 5, 241-246
14. Adams, M. J., Baker, E. N., Blundell, T. L., Harding, M. M., Dodson, E. J., Hodgkin, D. C., Dodson, G. G., Rimmer, B., Vijayan, M., and Sheat, S. (1969) Nature 224, 491-495
15. Kaarsholm, N. C., Ko, H. C., and Dunn, M. F. (1989) Biochemistry 28, 4427-4435
16. Choi, W. E., Brader, M. L., Aguilar, V., Kaarsholm, N. C., and Dunn, M. F. (1993) Biochemistry 32, 11638-11645
17. Brzovic, P. S., Choi, W.-J. E., Borchardt, D., Kaarsholm, N. C., and Dunn, M. F. (1994) Biochemistry 33, 13057-13069
18. Bloom, C. R., Choi, W.-J. E., Brzovic, P. S., Ha, J. J., Huang, S. T., Kaarsholm, N. C., and Dunn, M. F. (1995) J. Mol. Biol. 245, 324-330
19. Baker, E. N., Blundell, T. L., Cutfield, J. F., Cutfield, S. M., Dodson, E. J., Dodson, G. G., Hodgkin, D. M. C., Hubbard, R. E., Isaacs, N. W., Reynolds, C. D., Sakabe, K., Sakabe, N., and Vijayan, N. M. (1988) Philos. Trans. R. Soc. Land. Biol. Sci. B. 319, 369-456
20. Smith, G. D., Swenson, D. C., Dodson, E. J., Dodson, G. G., and Reynolds, C. D. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 7093-7097
21. Smith, G. D., and Dodson, G. G. (1992) Biopolymers 32, 441-445
22. Brader, M. L., Kaarsholm, N. C., Lee, W., and Dunn, M. F. (1991) Biochemistry 30, 6636-6645
23. Coleman, J. E., and Coleman, R. V. (1972) J. Biol. Chem. 247, 4718-4728
24. Holt, E. M., Holt, S. L., and Watson, K. J. (1970) J. Am. Chem. Soc. 92, 2721-2724
25. Lever, A. B. P. (1984) Inorganic Electronic Spectroscopy, 2nd Ed., pp. 196-198, Elsevier Science Publishing Co., Inc., New York
26. Bertini, I., Canti, G., Luchinat, C., and Scozzafava, A. (1978) J. Am. Chem. Soc. 100, 4873-4877
27. Smith, G. D., and Ciszak, E. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 8851-8855
28. Whittingham, J. L., Chaudhuri, S., Dodson, E. J., Moody, P. C. E., and Dodson, G. G. (1995) Biochemistry 34, 15553-15563
29. Ciszak, E., and Smith, G. D. (1994) Biochemistry 33, 1512-1517
30. Kaden, T. A., Holmquist, B., and Vallee, B. L. (1974) Inorg. Chem. 13, 2585-2590
31. Corwin, D. T., Gruff, E. S., and Koch, S. A. (1987) J. Chem. Soc., Chem. Commun. 13, 966-967
32. Thompson, J. S., Sorrel, T., Marks, T. J., and Ibers, J. A. (1979) J. Am. Chem. Soc. 101, 4193-4200
33. Brader, M. L., Kaarsholm, N. C., and Dunn, M. F. (1990) J. Biol. Chem. 265, 15666-15670
34. Eriksson, A. E., Jones, T. A., Kylsten, P. M., and Liljas, A. (1988) Proteins Struct. Funct. Genet. 4, 283-293
35. Lindskog, S. (1963) J. Biol. Chem. 238, 945-951
36. Hirose, J., Noji, M., and Kidane, Y. (1984) Chem. Pharm. Bull. 32, 2481-2485
37. Simonsson, I., Jonsson, B., and Lindskog, S. (1982) Biochem. Biophys. Res. Commun. 108, 1406-1412
38. Nair, S. K., Ludwig, P. A., and Christianson, D. W. (1994) J. Am. Chem. Soc. 116, 3659-3660
39. Baldwin, G. S., Galdes, A., Hill, H. A. O., Waley, S. G., and Abraham, E. P. (1980) J. Inorg. Biochem. 13, 189-204
40. McMillin, D. R., Holwerda, R. A., and Gray, H. B. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 1339-1341
41. McMillin, D. R., Rosenberg, R. C., and Gray, H. B. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 4760-4762
42. Solomon, E. I., Baldwin, M. J., and Lowery, M. D. (1992) Chem. Rev. 91, 521-541
43. Brader, M. L., Borchardt, D., and Dunn, M. F. (1992) J. Am. Chem. Soc. 114, 4480-4486
44. Brader, M. L., Borchardt, D., and Dunn, M. F. (1992) Biochemistry 31, 4691-4696
45. Storm, M. C., and Dunn, M. F. (1985) Biochemistry 24, 1749-1756
46. Roy, M., Brader, M. L., Lee, R. W.-K., Kaarsholm, N. C., Hansen, J., and Dunn, M. F. (1989) J. Biol. Chem. 264, 19081-19085