Solution structure of Co·Bleomycin A2 green complexed with d(CCAGGCCTGG)

Journal of the American Chemical Society

Volumn 118, Issue 6, 1996, Pages 1281-1294

  Wu, Wei ^a   Vanderwall, Dana E ^b   Turner, Christopher J ^c   Kozarich, John W ^b,d   Stubbe, Joanne ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b Bldg 142   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BLEOMYCIN A2 COBALT; BLEOMYCIN DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; DNA BINDING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE;

EID: 0029670556     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja952497w     Document Type: Article

References (68)

1. (a) Sikic, B. I., Rozencweig, M., Carter, S. K., Eds. In Bleomycin Chemotherapy, Academic Press: Orlando, FL. 1985.
2. (b) Umezawa, H. In Anticancer agents based on natural product models: Cassady, J. M., Douros, J., Eds.; Academic Press, Inc.: New York, 1980; Vol. 16, pp 147-166.
3. (c) Hecht, S. M. Ed. In Bleomycin: Chemical, Biochemical, and Biological Aspects; Springer-Verlag: New York, 1979.
4. Stubbe, J.; Kozarich, J. W. Chem. Rev. 1987, 87, 1107-1136.
5. Kane, S. A.; Hecht, S. M. In Progress in Nucleic Acid Research and Molecular Biology: Cohn, W. E., Moldave, K., Eds.: Academic Press: San Diego, CA, 1994; Vol. 49, pp 313-352.
6. Akkerman, M. A. J.; Haasnoot, C. A. G.; Hilbers, C. W. Eur. J. Biochem. 1988, 173, 211-225.
7. Akkerman, M. A. J.; Neijman, E. W. J. F.; Wijmenga, S. S.; Hilbers, C. W.; Bermel, W. J. Am. Chem. Soc. 1990, 112, 7462-7474.
8. Xu, R. X.; Nettesheim, D.; Otvos, J. D.; Petering, D. H. Biochemistry 1994, 33, 907-916.
9. Wu, W.; Vanderwall, D. E.; Lui, S. M.; Tang, X.-J.; Turner, C. J.; Kozarich, J. W.; Stubbe, J. J. Am. Chem. Soc. 1996, 118, 1268-1280 (preceding paper in this issue).
10. Gamesik, M. P.; Glickson, J. D.; Zon, G. J. Biomol. Struct. Dyn. 1990, 7, 1117-1133.
11. Hiroaki, H.; Nakayama, T.; Ikehara, M.; Uesugi, S. Chem. Pharm. Bull. 1991, 39, 2780-2786.
12. (a) Manderville, R. A.; Ellena, J. F.; Hecht, S. M. J. Am. Chem. Soc. 1994, 116, 10851-10852.
13. (b) Manderville, R. A.; Ellena, J. F.; Hecht, S. M. J. Am. Chem. Soc. 1995, 117, 7891-7903.
14. Chang, C.-H.; Meares, C. F. Biochemistry 1984, 23, 2268-2274.
15. Chang, C.-H.; Meares, C. F. Biochemistry 1982, 21, 6332-6334.
16. Burger, R. M.; Peisach, J.; Horwitz, S. B. J. Biol. Chem. 1981, 256, 11636-11644.
17. Xu, R. X.; Antholine, W. E.; Petering, D. H. J. Biol. Chem. 1992, 267, 950-955.
18. Wu, W.; Vandenvall, D. E.; Stubbe, J.; Kozarich, J. W.; Turner, C. J. J. Am. Chem. Soc. 1994, 116, 10843-10844.
19. (a) Boger, D. L.; Colletti, S. L.; Honda, T.; Menezes, R. F. J. Am. Chem. Soc. 1994, 116, 5607-5618.
20. (b) Boger, D. L.; Honda, T.; Dand, Q. J. Am. Chem. Soc. 1994, 116, 5619-5630.
21. (c) Boger, D. L.; Honda, T.; Menezes, R. F.; Colletti, S. L. J. Am. Chem. Soc. 1994, 116, 5631-5646.
22. (d) Boger, D. L.; Honda, T. J. Am. Chem. Soc. 1994, 116, 5647-5656.
23. Chang, C.-H.; Dallas, J. L.; Meares, C. F. Biochem. Biophys. Res. Commun. 1983, 110, 959-966.
24. Guéron, M.; Plateau, P.; Decorps, M. Prog. Nucl. Magn. Reson. Spectrosc. 1991, 23, 161.
25. Bax, A.; Subramanian, S. J. Magn. Reson. 1986, 67, 565-569.
26. Maudsley, A. A.; Ernst, R. R. Chem. Phys. Lett. 1977, 50, 368-372.
27. van Gunsteren, W. F.; Berendsen, H. J. C. Mol. Phys. 1977, 34, 1311-1327.
28. Brooks, B. R.; Bruccoleri, R. E.; Olafson, B. D.; States, D. J.; Swaminathan, S.; Karplus, M. J. Comput. Chem. 1983, 4, 187-217.
29. Manning, G. S. Q. Rev. Biophys. 1978, 11, 179-246.
30. Evans, S. V. J. Mol. Graphics 1993, 11, 134-138.
31. Haasnoot, C. A. G.; De Leeuw, F. A. A. M.; Altona, C. Tetrahedron 1980, 36, 2783-2792.
32. Dickerson, R. E. Methods Enzymol. 1992, 211, 67-111.
33. 2O ligand has replaced the hydroperoxide ligand) demonstrate that it binds 1 in an analogous fashion to CoBLM A2 green. The exchangeable proton, however, at 8.89 ppm is absent.
34. Wüthrich, K. NMR of Proteins and Nucleic Acids: John Wiley & Sons, Inc: New York, 1986.
35. (a) Majumdar, A.; Hosur, R. V. Prog. NMR Spectrosc. 1992, 24, 109.
36. (b) Hosur, R. V.; Ravikumar, M.; Chary, K. V. R.; Sheth, A.; Govil, G.; Zu-Kum, T.; Miles, H. T. FEBS 1986, 205, 71-76.
37. (c) van Wijk, J.; Huckriede, B. D.; Ippel, J. H.; Altona, C. Methods Enzymol. 1992, 211, 286-306.
38. Leupin, W.; Wagner, G.; Denny, W. A.; Wüthrich, K. Nucleic Acids Res. 1987, 15, 267-275.
39. (a) Gao, X.; Patel, D. J. Biochemistry 1988, 27, 1744-1751.
40. (b) Addess, K. J.; Gilbert, D. E.; Olsen, R. K.; Feison, J. Biochemistry 1992, 31, 339-350.
41. Gorenstein, D. G. Methods Enzymol. 1992, 211, 254-286.
42. Kim, S.; Lin, L.; Reid, B. R. Biochemistry 1992, 31, 3564-3574.
43. (a) Dickerson, R. E. In Mechanism of DNA Damage and Repair: Implications for Carcinogenesis and Risk Assessment Basic Life Sciences; Smi, M. G., Grossman, L., Eds., Plenum: New York, 1986; Vol. 38, pp 245-255.
44. (b) Klevit, R. E.; Wemmer, D. E.; Reid, B. R. Biochemistry 1986, 25, 3296.
45. Kuwahara, J.; Sugiura, Y. Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 2459-2463.
46. 7 (Figure 7c).
47. Povirk, L. F.; Hogan, M.; Dattagupta, N. Biochemistry 1979, 18, 96-101.
48. Williams, L. D.; Goldberg, I. H. Biochemistry 1988, 27, 3004-3011.
49. (a) Although the penultimate thiazolium ring as a whole is partially stacked between the bases of C6 and C7, the B-H5′ proton is positioned almost directly below the base of C6, which causes the upfield chemical shift change (0.61 ppm) due to the ring current effect. The B-H5 proton is completely stacked between G14 and G15 (Figure 9) and thus experiences even larger upfield chemical shift change (0.91 ppm). (b) The bithiazole tail is sufficiently flexible in the free CoBLM A2 green such that the orientation of the thiazolium rings relative to one another is not discernible.
50. (a) Tsai, C.; Jain, S C.; Sobell, H. M. J. Mol. Biol. 1977, 114, 301-305.
51. (b) Tsai, C.; Jain, S. C.; Sobell, H. M. J. Mol. Biol. 1977, 114, 317-331.
52. Williams, L. D.; Egli, M;: Gao, Q.; Rich, A. DNA Intercalation: Helix Unwinding and Neighbor-Exclusion; Adenine Press: Schenectady, NY, 1992.
53. (a) Frederick, C. A.; Williams, L. D.; Ughetto, G.; van der Marel, G. A.; van Boom, J. H.; Rich, A., Wang, A. H. Biochemistry 1990, 29, 2538-2549.
54. (b) Gao, Y., Liaw, Y.; Robinson, H.; Wang, A. H. Biochemistry 1990, 29, 10307-10316.
55. (a) Carter, B. J.; Murty, V. S.; Reddy, K. S.; Wang, S.-N.; Hecht, S. M. J. Biol. Chem. 1990, 265, 4193-4196.
56. (b) Carter, B. J.; Reddy, K. S.; Hecht, S. M. Tetrahedron 1991, 47, 2463-2474.
57. Levy, M. J.; Hecht, S. M. Biochemistry 1988, 27, 2647-2650.
58. Zhang, G. Ph.D. Thesis, University of Maryland, 1993.
59. The H bond distance is between the proton and the H bond acceptor atom in all cases. The H bond angle is determined by the donor atom, the hydrogen, and the acceptor atom.
60. Guajardo, R. J.; Hudson, S. E.; Brown, S. J.; Mascharak, P. K. J. Am. Chem, Soc. 1993, 115, 7971-7977.
61. (a) Boser, D. L.; Teramoto, S.; Honda, T.; Zhou, J. J. Am. Chem. Soc. 1995, 117, 7338-7343.
62. (b) Boser, D. L.; Teramoto, S.; Zhou, J. J. Am. Chem. Soc. 1995, 117, 7344-7356.
63. (c) Boger, D. L.; Colletti, S. L.; Teramoto, S.; Ramsey, T. M.; Zhou, J. Bioorg. Med. Chem. 1995, 3, 1281-1295.
64. English, A. M.; Tsaprailis, G. Adv. Inorg. Chem. 1995, in press.
65. (a) Absalon, M. J.; Stubbe, J.; Kozarich, J. W. Biochemistry 1995, 34, 2065-2075.
66. (b) Absalon, M. J.; Wu, W., Stubbe, J.; Kozarich, J. W. Biochemistry 1995, 34, 2076-2086.
67. Povirk, L. F.; Han, Y.-H.; Steighner, R. J. Biochemistry 1989, 28, 5808-5814.
68. Loeb, K. E.; Zaleski, J. M.; Westre, T. E.; Guajardo, R. J.; Mascharak, P. K.; Hedman, B.; Hodgson, K. O.; Solomon, E. I. J. Am. Chem. Soc. 1995, 117, 4545-4561.