Origin of the anomalous Fe-CO stretching mode in the CO complex of Ascaris hemoglobin

Biochemistry

Volumn 39, Issue 4, 2000, Pages 837-842

  Das, Tapan Kanti ^a   Friedman, Joel M ^a   Kloek, Andrew P ^b   Goldberg, Daniel E ^b   Rousseau, Denis L ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; GLUTAMINE; HEMOGLOBIN; IRON; MYOGLOBIN; OXYGEN; TYROSINE;

ARTICLE; ASCARIS; CHEMICAL BOND; HYDROGEN BOND; MOLECULAR MODEL; OXYGEN TRANSPORT; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; ASCARIS SUUM; CARBON MONOXIDE; HEMOGLOBINS; IRON; OXIDOREDUCTASES; PHENYLALANINE; PROTEIN CONFORMATION; SPECTRUM ANALYSIS, RAMAN; TYROSINE;

ASCARIS; ASCARIS SUUM; CETACEA; OXY; PHYSETER CATODON; VERTEBRATA;

EID: 0034141829     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9922087     Document Type: Article

References (35)

1. Hardison, R. (1998) Hemoglobins from bacteria to man: evolution of different patterns of gene expression, J. Exp. Biol. 201, 1099-1117.
2. Crawford, M. J., and Goldberg, D. E. (1998) Role for the Salmonella flavohemoglobin in protection from nitric oxide, J. Biol. Chem. 273, 12543-12547.
3. Gardner, P. R., Gardner, A. M., Martin, L. A., and Salzman, A. L. (1998) Nitric oxide dioxygenase: an enzymic function for flavohemoglobin, Proc. Natl. Acad. Sci. U.S.A. 95, 10378-10383.
4. Hausladen, A., Gow, A. J., and Stamler, J. S. (1998) Nitrosative stress: metabolic pathway involving the flavohemoglobin, Prac. Natl. Acad. Sci. U.S.A. 95, 14100-14105.
5. Minning, D. M., Gow, A. J., Bonaventura, J., Braun, R., Dewhirst, M., Goldberg, D. E., and Stamler, J. S. (1999) Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase', Nature 401, 497-502.
6. Das, T. K., Couture, M., Lee, H. C., Peisach, J., Rousseau, D. L., Wittenberg, B. A., Wittenberg, J. B., and Guertin, M. (1999) Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme, Biochemistry 38, 15360-15368.
7. Arredondo-Peter, R., Hargrove, M. S., Moran, J. F., Sarath, G., and Klucas, R. V. (1998) Plant hemoglobins, Plant Physiol. 118, 1121-1125.
8. Membrillo-Hernandez, J., Coopamah, M. D., Anjum, M. F., Stevanin, T. M., Kelly, A., Hughes, M. N., and Poole, R. K. (1999) The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "Nitric oxide Releaser," and paraquat and is essential for transcriptional responses to oxidative stress, J. Biol. Chem. 274, 748-754.
9. Sowa, A. W., Duff, S. M. G., Guy, P. A., and Hill, R. D. (1998) Altering hemoglobin levels changes energy status in maize cells under hypoxia, Proc. Natl. Acad. Sci. U.S.A. 95, 10317-10321.
10. Das, T. K., Lee, H. C., Duff, S. M., Hill, R. D., Peisach, J., Rousseau, D. L., Wittenberg, B. A., and Wittenberg, J. B. (1999) The heme environment in barley hemoglobin, J. Biol. Chem. 274, 4207-4212.
11. 2 and NO, in Biological Applications of Roman Spectroscope (Spiro, T. G., Ed.) Vol. 3, pp 39-95, John Wiley & Sons, New York.
12. Li, X.-Y., and Spiro, T. G. (1988) Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data, J. Am. Chem. Soc. 110, 6024-6033.
13. Ray, G. B., Li, X.-Y., Ibers, J. A., Sessler, J. L., and Spiro, T. G. (1994) How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models, J. Am. Chem. Soc. 116, 162-176.
14. Morikis, D., Champion, P. M., Springer, B. A., and Sligar, S. G. (1989) Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement, Biochemistry 28, 4791-4800.
15. Lin, S. H., Yu, N. T., Tame, J., Shih, D., Renaud, J. P., Pagnier, J., and Nagai, K. (1990) Effect of the distal residues on the vibrational modes of the Fe-CO bond in hemoglobin studied by protein engineering, Biochemistry 29, 5562-5566.
16. Ling, J., Li, T., Olson, J. S., and Bocian, D. F. (1994) Identification of the iron-carbonyl stretch in distal histidine mutants of carbonmonoxymyoglobin, Biochim. Biophys. Acta 1188, 417-421.
17. Li, T., Quillin, M. L., Phillips, G. N., Jr., and Olson, J. S. (1994) Structural determinants of the stretching frequency of CO bound to myoglobin, Biochemistry 33, 1433-1446.
18. Phillips, G. N., Jr., Teodoro, M. L., Li, T., Smith, B., and Olson, J. S. (1999) Bound CO as a molecular probe of electrostatic potential in the distal pocket of myoglobin, J. Phys. Chem. B 103, 8817-8829.
19. Sakan, Y., Ogura, T., Kitagawa, T., Fraunfelter, F. A., Mattera, R., and Ikeda-Saito, M. (1993) Time-resolved resonance Raman study on the binding of carbon monoxide to recombinant human myoglobin and its distal histidine mutants, Biochemistry 32, 5815-5824.
20. Anderton, C. L., Hester, R. E., and Moore, J. N. (1997) A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity, Biochim. Biophys. Acta 1338, 107-120.
21. Davenport, H. E. (1949) The haemoglobins of Ascaris lumbricoides, Proc. R. Soc. London B 136, 255-270.
22. Okazaki, T., and Wittenberg, J. B. (1965) The hemoglobin of Ascaris perienteric fluid. 3. Equilibria with oxygen and carbon monoxide, Biochim. Biophys. Acta 111, 503-511.
23. Gibson, Q. H., and Smith, M. H. (1965) Rates of reaction of Ascaris haemoglobins with ligands, Proc. R. Soc. London B 163, 206-214.
24. Springer, B. A., Egeberg, K. D., Sugar, S. G., Rohlfs, R. J., Mathews, A. J., and Olson, J. S. (1989) Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myoglobin. Site-directed mutagenesis of the distal histidine, J. Biol. Chem. 264, 3057-3060.
25. Wittenberg, J. B. (1966) The molecular mechanism of hemoglobin-facilitated oxygen diffusion, J. Biol. Chem. 241, 104-114.
26. Yang, J., Kloek, A. P., Goldberg, D. E., and Mathews, F. S. (1995) The structure of Ascaris hemoglobin domain I at 2.2 Å resolution: molecular features of oxygen avidity, Proc. Natl. Acad. Sci. U.S.A. 92, 4224-4228.
27. Kloek, A. P., Yang, J., Mathews, F. S., Frieden, C., and Goldberg, D. E. (1994) The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin, J. Biol. Chem. 269, 2377-2379.
28. De Baere, I., Perutz, M. F., Kiger, L., Marden, M. C., and Poyart, C. (1994) Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin, Proc. Natl. Acad. Sci. U.S.A. 91, 1594-1597.
29. Travaglini Allocatelli, C., Cutruzzola, F., Brancaccio, A., Vallone, B., and Brunori, M. (1994) Engineering Ascaris hemoglobin oxygen affinity in sperm whale myoglobin: role of tyrosine B10, FEBS Lett. 352, 63-66.
30. Huang, S., Huang, J., Kloek, A. P., Goldberg, D. E., and Friedman, J. M. (1996) Hydrogen bonding of tyrosine B10 to heme-bound oxygen in Ascaris hemoglobin. Direct evidence from UV resonance Raman spectroscopy, J. Biol. Chem. 271, 958-962.
31. Peterson, E. P., Huang, S., Wang, J., Miller, L. M., Vidugiris, G., Kloek, A. P., Goldberg, D. E., Chance, M. R., Wittenberg, J. B., and Friedman, J. M. (1997) A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata). Biochemistry 36, 13110-13121.
32. Unno, M., Christian, J. F., Olson, J. S., Sage, J. T., and Champion, P. M. (1998) Evidence for hydrogen bonding effects in the iron ligand vibrations of carbonmonoxymyoglobin, J. Am. Chem. Soc. 120, 2670-2671.
33. Kushkuley, B., and Stavrov, S. S. (1996) Theoretical study of the distal-side steric and electrostatic effects on the vibrational characteristics of the FeCO unit of the carbonylheme proteins and their models, Biophys. J. 70, 1214-1229.
34. Zhao, X., Vyas, K., Nguyen, B. D., Rajarathnam, K., La Mar, G. N., Li, T., Phillips, G. N., Jr., Eich, R. F., Olson, J. S., Ling, J., and Bocian, D. F. (1995) A double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobin, J. Biol. Chem. 270, 20763-20774.
35. 2 Raman bands for oxymyoglobin mutants, J. Am. Chem. Soc. 118, 7845-7846.