Substitution of the heme binding module in hemoglobin α- and β- subunits. Implication for different regulation mechanisms of the heme proximal structure between hemoglobin and myoglobin

Journal of Biological Chemistry

Volumn 275, Issue 17, 2000, Pages 12438-12445

  Inaba, Kenji ^a,c   Ishimori, Koichiro ^a   Imai, Kiyohiro ^b   Morishima, Isao ^a  

^a KYOTO UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

^c MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN; MYOGLOBIN; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; GEL CHROMATOGRAPHY; HEMOGLOBIN DETERMINATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; REGULATORY MECHANISM; STRUCTURE ANALYSIS;

CHROMATOGRAPHY, GEL; ESCHERICHIA COLI; HEME; HEMOGLOBINS; MAGNETIC RESONANCE SPECTROSCOPY; MYOGLOBIN; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTRUM ANALYSIS, RAMAN;

EID: 0034725116     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.17.12438     Document Type: Article

References (70)

1. Adachi, S., Sunohara, N., Ishimori, K., and Morishima, I. (1992) J. Biol. Chem. 267, 12614-12621
2. Uchida, T., Ishimori, K., and Morishima, I. (1997) J. Biol. Chem. 272, 30108-30114
3. Matsui, T., Ozaki, S., Liong, E., Phillips, G. N., Jr., and Watanabe, Y. (1999) J. Biol. Chem. 274, 2838-2844
4. Tanaka, M., Ishimori, I., and Morishima, I. (1999) Biochemistry 38, 10463-10473
5. Poulos, T. L., Freer, S. T., Alden, R. A., Edwards, S. L., Skogland, U., Takio, K., Errikson, B., Xuong, N., Yonetani, T., and Kraut, J. (1980) J. Biol. Chem. 255, 575-583
6. Oldfield, T. J., Smerdon, S. J., Dauter, Z., Petratos, K., Wilson, K. S., and Wilkinson, A. J. (1992) Biochemistry 31, 8732-8739
7. Smerdon, S. J., Krzywda, S., and Wilkinson, A. J. (1993) Biochemistry 32, 5132-5138
8. Adachi, S., Nagano, S., Ishimori, K., Watanabe, Y., and Morishima, I. (1991) Biochem. Biophys. Res. Commun. 180, 138-144
9. Adachi, S., Nagano, S., Ishimori, K., Watanabe, Y. Egawa, T., Kitagawa, T., Makino, R., and Morishima, I. (1993) Biochemistry 32, 241-252
10. Hildebrand, D. P., Burk, D. L., Maurus, R., Ferrer, J. C., Brayer, G. D., and Mauk, A. G. (1995) Biochemistry 34, 1997-2005
11. Matsui, T., Nagano, S., Ishimori, K., Watanabe, Y., and Morishima, I. (1996) Biochemistry 35, 13118-13124
12. Poulos, T. L. (1996) J. Biol. Inorg. Chem. 1, 356-359
13. Inaba, K., Ishimori, K., and Morishima, I. (1998) J. Mol. Biol. 283, 311-327
14. Go, M. (1981) Nature 291, 90-92
15. Wakasugi, K., Ishimori, K., Imai, K., Wada, Y., and Morishima, I. (1994) J. Biol. Chem. 269, 18750-18756
16. Wakasugi, K., Inaba, K., Ishimori, K., and Morishima, I. (1997) Biophys. Chem. 68, 265-273
17. Inaba, K., Wakasugi, K., Ishimori, K. Konno, T. Kataoka, M., and Morishima, I. (1997) J. Biol. Chem. 272, 30054-30060
18. Inaba, K., Ishimori, K., Imai, K., and Morishima, I. (1998) J. Biol. Chem. 273, 8080-8087
19. Jellie, A. M., Tate, W. P., and Trotman, C. N. A. (1996) J. Mol. Evol. 42, 641-647
20. Nagai, K and Thøgerson, H. C. (1984) Nature 309, 810-812
21. Nagai, K., Perutz, M. F., and Poyart, C. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 7252-7257
22. Wada, T., Fujita, T., Hayashi, A., Sakurai, T., and Matsuo, T. (1989) Biomed. Environ. Mass Spectrom. 18, 563-565
23. Valdes, R., Jr., and Ackers, G. K. (1977) J. Biol. Chem. 252, 74-81
24. Ishimori, K., Hashimoto, M., Imai, K., Fushitani, K., Miyazaki, G., Morimoto, H., Wada, Y., and Morishima, I. (1994) Biochemistry 33, 2546-2553
25. Piotto, M., Saudek, V., and Sklenar, V. (1992) J. Biomol. NMR 2, 661-666
26. Imai, K. (1981) Methods Enzymol. 76, 438-449
27. Imai, K. (1982) Allosteric Effect in Haemoglobin, Cambridge University Press, Cambridge, UK
28. Imai, K., Morimoto, H., Kotani, M., Watari, H., Hitata, W., and Kuroda, M. (1970) Biochim. Biophys. Acta 200, 189-196
29. Hayashi, A., Suzuki, T., and Shin, M. (1973) Biochim. Biophys. Acta 310, 309-316
30. Lynch. R. E., Lee, E., and Cartwright, G. E. (1976) J. Biol. Chem. 281, 1015-1019
31. Winterbourn, C. C., McGrath, B. M., and Carrell, R. W. (1976) Biochem. J. 155, 493-502
32. Imai, K. (1994) Methods Emymol. 232, 559-576
33. Lindstrom, T. R., Nore, I. B. E., Charashe, S., Lehmann, H., and Ho, C. (1972) Biochemistry 11, 1677-1681
34. Nagai, K., La Mar, G. N., Jue, T., and Bunn, H. F., (1982) Biochemistry 21, 842-847
35. Fung, L. W. M., and Ho, C. (1975) Biochemistry 14, 2526-2535
36. Russu, I. M., Ho, N. T., and Ho, C. (1987) Biochim. Biophys. Acta 914, 40-48
37. Asakura, T., Adachi, K., Wiley, J. S., Fung, L W.-M., Ho, C., Kilmartin, J. V., and Perutz, M. F. (1976) J. Mol. Biol. 104, 185-195
38. Ishimori, K., Imai, K., Miyazaki, G., Kitagawa, T., Wada, Y., Morimoto, H., and Morishima, I. (1992) Biochemistry 31, 3256-3262
39. Takahashi, S., Lin, A. K. -L. C., and Ho, C. (1980) Biochemistry 19, 5196-5202
40. Ho, C. (1992) Adv. Protein Chem. 43, 153-312
41. Nagai, K., Kitagawa, T., and Morimoto, H. (1980) J. Mol. Biol. 136, 271-289
42. Nagai, K., and Kitagawa, T. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 2033-2037
43. Dalvit, C., and Ho, C. (1985) Biochemistry 24, 3398-3407
44. Shulman, R. G., Wuthrich, K., Yamane, T., Patel, D., and Blumnberg, W. E. (1970) J. Mol. Biol. 53, 143-157
45. La Mar (1979) in Biological Applications of Magnetic Resonances (Shulman, R. G., ed) pp. 305-342, Academic Press, Inc., New York
46. La Mar, G. N., Yamamoto, Y., Jue, T., Smith, K. M., and Pandey, R. K. (1985) Biochemistry 24, 3826-3831
47. Ishimori, K., and Morishima, I. (1988) Biochemistry 27, 4747-4753
48. Yamamoto, Y., and La Mar, G. N. (1986) Biochemistry 25, 5288-5297
49. La Mar, G. N., Jue, T., Nagai, K., Smith, K. M., Yamamoto, Y., Kauten, R. J., Thanabal, V., Langry, K. C., Pandey, R. K., and Leung, H-K. (1988) Biochim. Biophys. Acta 952, 131-141
50. Eliezer, D and Wright, P. E. (1996) J Mol. Biol. 263, 531-538
51. Lim, V. I., and Efimov, A. V. (1977) FEBS Lett. 78, 279-283
52. Leutzinger, Y., and Beychok, S. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 780-784
53. Borgstahl, G. E. O., Rogers, P. H., and Arnone, A. (1994) J. Mol. Biol. 236, 831-843
54. Perutz, M. F. (1970) Nature 228, 726-739
55. Perutz, M. F. (1989) Q. Rev. Biophys. 22, 139-226
56. Barrick, D., Ho, N. T., Simplaceanu, V., Dahlquist, F. W., and Ho, C. (1997) Nat. Struct. Biol. 4, 78-83
57. Dayhoff, M. O. (1972) Atlas of Protein Sequence and Structure, Vol. 5, National Biomedical Research Foundation, Washington, D. C.
58. Imai, K., Fushitani, K., Miyazaki, Z., Ishimori, K., Kitagawa, T., Wada, Y., Morimoto, H., Morishima, I., Shih, D. T., and Tame, J. (1991) J. Mol. Biol. 218, 769-778
59. Hashimoto, M., Ishimori, K., Imai, K., Miyazaki, G., Morimoto, H., Wada, Y., and Morishima, I. (1993) Biochemistry 32, 13688-13695
60. Adachi, K., Vonk, H., Reilly, M. P., Adachi, H., Schroeder, W. A., Schwartz, E., and Asakura, T. (1984) Biochim. Biophys. Acta 790, 132-140
61. Shih, D. T., Jones, R. T., Imai, K., and Tyuma, I. (1985) J. Biol. Chem 260, 5919-5924
62. Smith, L. L., Plese, C. F., Barton, B. P., Charache, S., Wilson, J. B., and Huisman, T. H. J. (1972) J. Biol. Chem. 247, 1433-1439
63. Sasaki, J., Imamura, T., Yanase, T., Atha, D. H., Riggs, A. (1978) J. Biol. Chem. 253, 87-94
64. Eaton, W. A. (1980) Nature 284, 183-185
65. Schaeffer, C., Craescu, C. T., Mispelter, J., Garel, M. -C., Rosa, J., and Lhoste, J.-M. (1988) Eur. J. Biochem. 173, 317-325
66. Craescu, C. T., and Mispelter, J. (1988) Eur. J Biochem. 176, 171-178
67. Noguti, T., Sakakibara, H., and Go, M. (1993) Proteins 16, 357-363
68. Go, M., and Noguti, T. (1995) Tracing Biological Evolution in Protein and Gene Structures (Go, M. and Shimmel, P., eds) pp. 229-235, Elsevier Science Publishers B. V., Amsterdam
69. Ryrie, D. R., Plowman, D., and Lehmann, H. (1977) FEBS Lett. 83, 260-262
70. Williamson, D., Beresford, C. H., Langdown, J. V., Anderson, C. C., and Green, A. R. (1994) Br. J. Haematol. 86, 890-892