Heme speciation in alkaline ferric FixL and possible tyrosine involvement in the signal transduction pathway for regulation of nitrogen fixation

Biochemistry

Volumn 37, Issue 39, 1998, Pages 13543-13552

  Lukat Rodgers, Gudrun S ^a   Rexine, Joey L ^a   Rodgers, Kenton R ^a  

^a NORTH DAKOTA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDE; FERRIC ION; HEME; HEMOGLOBIN; HYDROXIDE; MYOGLOBIN; PHOSPHOTRANSFERASE; TYROSINE;

ALKALINITY; ARTICLE; ELECTRON SPIN RESONANCE; NITROGEN FIXATION; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; SINORHIZOBIUM MELILOTI; ULTRAVIOLET SPECTROSCOPY;

BACTERIAL PROTEINS; FERRIC COMPOUNDS; HEME; HEMEPROTEINS; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; LIGANDS; NITROGEN FIXATION; PEPTIDE FRAGMENTS; PHOSPHOTRANSFERASES; SIGNAL TRANSDUCTION; SINORHIZOBIUM MELILOTI; SPECTROPHOTOMETRY, ULTRAVIOLET; TYROSINE;

OXY; RHIZOBIUM; SINORHIZOBIUM MELILOTI;

EID: 0032578444     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981439v     Document Type: Article

References (55)

1. He, Y., Shelver, D., Kerby, R. L., and Roberts, G. P. (1996) J. Biol. Chem. 271, 120-123.
2. Aono, S., Hakajima, H., Saito, K., and Okada, M. (1996) Biochem. Biophys. Res. Commun. 228, 752-756.
3. Garber, D. L., and Lowe, D. G. (1994) J. Biol. Chem. 269, 30741-30744.
4. Gilles-Gonzales, M. A., Gonzalez, G., Perutz, M. F., Kiger, L., Marden, M. C., and Poyrart, C. (1994) Biochemistry 33, 8067-8073.
5. David, M., Daveran, M. L., Batut, J., Dedieu, A., Domergue, O., Ghai, J., Hertig, C., Boistard, P., and Kahn, D. (1988) Cell 54, 671-683.
6. Gilles-Gonzalez, M. A., Ditta, G. S., and Helinski, D. R. (1991) Nature 350, 170-172.
7. Monson, E. K., Weinstein, M., Ditta, G. S., and Helinski, D. R. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 4280-4284.
8. Lois, A. F., Weinstein, M., Ditta, G. S., and Helinski, D. R. (1993) J. Biol. Chem. 268, 4370-4375.
9. Agron, P. G., Ditta, G. S., and Helinski, D. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 3506-3510.
10. Reyrat, J., David, M., Blonski, C., Boistard, P., and Batut, J. (1993) J. Bacteriol. 175, 6867-6872.
11. Galinier, A., Garnerone, A., Reyrat J., Kahn, D., Batut, J., and Boistard, P. (1994) J. Biol. Chem. 269, 23784-23789.
12. Gilles-Gonzalez, M. A., Gonzalez, G., and Perutz, M. F. (1995) Biochemistry 34, 232-236.
13. Winkler, W. C., Gonzalez, G., Wittenberg, J. B., Hille, R., Dakappagari, N., Jacob, A., Gonzalez, L. A., and Gilles-Gonzalez, M. A. (1996) Chem. Biol. 3, 841-850.
14. Beetlestone, J., and George, P. (1964) Biochemistry 3, 707-714.
15. George, P., Beetlestone, J., and Griffith, J. S. (1964) Rev. Mod. Phys. 36, 441-455.
16. Asher, S. A., Vickery, L. E., Schuster, T. M., and Sauer, K. (1977) Biochemistry 16, 5849-5856.
17. Asher, S. A., and Schuster, T. M. (1979) Biochemistry 18, 5377-5387.
18. Desbois, A., Lutz, M., and Banerjee, R. (1979) Biochemistry 18, 1510-1518.
19. Feis, A., Marzocchi, M. P., Paoli, M., and Smulevich, G. (1994) Biochemistry 33, 4577-4583.
20. Sitter, A. J., Shifflett, J. R., and Terner, J. (1988) J. Biol. Chem. 263, 13032-13038.
21. Takahashi, S., Wang, J., Rousseau, D. L., Ishikawa, K., Yoshida, T., Host, J. R., and Ikeda-Saito, M. (1994) J. Biol. Chem. 269, 1010-1014.
22. Takahashi, S., Wang, J., Rousseau, D. L., Ishikawa, K., Yoshida, T., Takeuchi, N., and Ikeda-Saito, M. (1994) Biochemistry 33, 5531-5538.
23. Ishikawa, K., Takeuchi, N., Takahashi, S., Matera, K. M., Sato, M., Shibahara, S., Rousseau, D. L., Ikeda-Saito, M., and Yoshida, T. (1995) J. Biol. Chem. 270, 6345-6350.
24. Smulevich, G., Neri, F., Marzocchi, M. P., and Welinder, K. G. (1996) Biochemistry 35, 10576-10585.
25. Smulevich, G., Miller, M. A., Kraut, J., and Spiro, T. G. (1991) Biochemistry 30, 9546-9558.
26. Howes, B. D., Rodriguez-Lopez, J. N., Smith, A. T., and Smulevich, G. (1997) Biochemistry 36, 1532-1543.
27. Rodgers, K. R., Lukat-Rodgers, G. S., and Barron, J. A. (1996) Biochemistry 35, 9539-9548.
28. Lukat-Rodgers, G. S., and Rodgers, K. R. (1997) Biochemistry, 36, 4178-4187.
29. Antonini, E., and Brunori, M. Frontier in Biology; Hemoglobin and Myoglobin in Their Reactions with Ligands (1971) Vol. 21, North-Holland Publishing Co., Amsterdam.
30. Sun, J., Wilks, A., Ortiz de Montellano, P. R., and Loehr, T. M. (1993) Biochemistry 32, 14151-14157.
31. Monson, E. K., Ditta, G. S., and Helinski, D. R. (1995) J. Biol. Chem. 270, 5243-5250.
32. Rava, R. P., and Spiro, T. G. (1985) J. Phys. Chem. 89, 1856-1861.
33. Ludwig, M., and Asher, S. A. (1988) J. Am. Chem. Soc. 110, 1005-1011.
34. Makinen, M. W., and Churg, A. K. (1983) in Iron Porphyrins Part One (Lever, A. B. P., and Gray, H. B., Eds.) pp 141-236, Addison-Wesley, Reading, MA.
35. Drago, R. S. Physical Methods for Chemists, 2nd ed., pp 103-106, Surfside Scientific Publishers, Gainseville, FL.
36. Spiro, T. G., Stong, J. D., and Stein, P. (1979) J. Am. Chem. Soc. 101, 2648-2655.
37. Choi, S., Spiro, T. G., Langry, K. C., Smith, K. M., Budd, D. L., and LaMar, G. N. (1982) J. Am. Chem. Soc. 104, 4345-4351.
38. Lukat-Rodgers, G. S., and Rodgers, K. R. (1998) JBIC, J. Biol. Inorg. Chem. 3, 274-281.
39. Rousseau, D. L., Ching, Y., Brunori, M., and Giacometti, G. M. (1989) J. Biol. Chem. 264, 7878-7881.
40. Palaniappan, V., and Terner, J. (1989) J. Biol. Chem. 264, 16046-16053.
41. Smulevich, G., Mauro, J. M., Fishel, L. A., English, A. M., Kraut, J., and Spiro, T. G. (1988) Biochemistry 27, 5477-5485.
42. Spiro, T. G., and Li, X. Y. (1988) in Biological Aplications of Raman Spectroscopy (Spiro, T. G., Ed.) Vol. 3, pp 1-38, John Wiley & Sons, New York.
43. Palmer, G. (1985) Biochem. Soc. Trans. 13, 548-560.
44. Ikeda-Saito, M., Hori, H., Andersson, L. A., Prince, R. C., Pickering, I. J., George, G. N., Sanders, C. R., II, Lutz, R. S., McKelvey, E. J., and Mattera, R. (1992) J. Biol. Chem. 267, 22843-22852.
45. Bogumil, R., Maurus, R., Hildebrand, D. P., Brayer, G. D., and Mauk, A. G. (1995) Biochemistry 34, 10483-10490.
46. Peisach, J., Blumberg, W. E., Ogawa, S., Rachmilewitz, E. A., and Oltzik, R. (1971) J. Biol. Chem. 246, 3342-3355.
47. Krauss, D. W., Wittenberg, J. B., Jing-Fen, L., and Peisach, J. (1990) J. Biol. Chem. 265, 16054-16059.
48. Rotilio, G., Calabrese, L., Giacometti, G. M., and Brunori, M. (1971) Biochim. Biophys. Acta 236, 234-237.
49. Appleby, C. A., Blumberg, W. E., Peisach, J., Wittenberg, B. A., and Wittenberg, J. B. (1976) J. Biol. Chem. 251, 6090-6096.
50. Tamura, K., Nakamura, H., Tanaka, Y., Oue, S., Tsukamoto, K., Normura, M., Tsuchiya, T., Adachi, S., Takahashi, Iizuka, T., and Shiro, Y. (1996) J. Am. Chem. Soc. 118, 9434-9435..
51. Hu, S., Smith, K. M., and Spiro, T. G. (1996) J. Am. Che. Soc. 118, 12638-12646.
52. Smulevich, G., Hu, S., Rodgers, K. R., Goodin, D. B., Smith, K. M., and Spiro, T. G. (1996) Biospectroscopy 2, 365-376.
53. Hashimoto, S., Tatsuno, Y., and Kitagawa, T. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 2417-2422.
54. Hashimoto, S., Teraoka, J., Inubushi, T., Yonetani, T., and Kitagawa, T. (1986) J. Biol. Chem. 261, 11110-11117.
55. Teraoka, J., and Kitagawa, T. (1981) J. Biol. Chem. 256, 3969-3977.