Oxygen-Avid Hemoglobin of Ascaris

Chemical Reviews

Volumn 99, Issue 12, 1999, Pages 3371-3378

  Goldberg, Daniel E ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0345761151     PISSN: 00092665     EISSN: None     Source Type: Journal    
DOI: 10.1021/cr970152l     Document Type: Article

References (60)

1. Warren, K. The Biology of Parasitism; Liss: New York, 1988.
2. Crompton, D. The prevalence of ascariasis. Parasitol. Today 1988, 4, 162-164.
3. Sarinas, P.; Chitkara, R. Ascariasis and hookworm. Sem. Resp. Inf. 1997, 12, 130-137.
4. Oberhelman, R. A.; Guerrero, E. S.; Fernandez, M. L.; Silio, M.; Mercado, D.; Comiskey, N.; Ihenacho, G.; Mera, R. Correlation between intestinal parasitosis, physical growth, and psychomotor development among infants and children from rural Nicaragua. Am. J. Trop. Med. Hyg. 1998, 58, 470-475.
5. Khuroo, M. Ascariasis. Gastroenterol. Clin. N. Am. 1996, 25, 553-577.
6. Goldberg, D. The enigmatic oxygen-avid hemoglobin of Ascaris. Bioessays 1995, 17, 177-182.
7. Davenport, H. The haemoglobins of Ascaris lumbricoides. Proc. R. Soc. B 1949, 136, 255-270.
8. Okazaki, T.; Briehl, R. W.; Wittenberg, J. B.; Wittenberg, B. A. The hemoglobin of Ascaris perienteric fluid II. Molecular weight and subunits. Biochim. Biophys. Acta 1965, 111, 496-502.
9. Darawshe, S.; Tsafadyah, Y.; Daniel, E. Quaternary structure of erythrocruorin from the nematode Ascaris suum. Biochem. J. 1987, 242, 689-694.
10. Darawshe, S.; Daniel, E. Structure of the polypeptide chain of extracellular hemoglobin from the nematode Ascaris suum. Comp. Biochem. Physiol. 1991, 99B, 425-429.
11. Sherman, D. R.; Kloek, A. P.; Krishnan, R.; Guinn, B.; Goldberg, D. E. Ascaris hemoglobin gene: Plant-like structure reflects the ancestral globin gene. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 11696-11700.
12. De Baere, I.; Liu, L.; Moens, L.; Van Beeumen, J.; Gielens, C.; Richelle, J.; Trotman, C.; Finch, J.; Gerstein, M.; Perutz, M. Polar zipper sequence in the high-affinity hemoglobin of Ascaris suum: amino acid sequence and structural interpretation. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4638-4642.
13. Yang, J.; Kloek, A. P.; Goldberg, D. E.; Mathews, F. S. The structure of Ascaris hemoglobin domain I at 2.2A resolution: molecular features of oxygen avidity. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 4224-4228.
14. Darawshe, S.; Daniel, E. Molecular symmetry and arrangement of subunits in extracellular hemoglobin from the nematode Ascaris suum. Eur. J. Biochem. 1991, 201, 169-173.
15. Kloek, A. P.; Yang, J.; Mathews, F. S.; Goldberg, D. E. Expression, characterization, and crystallization of oxygen-avid Ascaris hemoglobin domains. J. Biol. Chem. 1993, 268, 17669-17771.
16. Perutz, M.; Staden, R.; Moens, L.; De Baere, I. Polar Zippers. Curr. Biology. 1993, 3, 249-253.
17. Minning, D. M.; Kloek, A. P.; Yang, J.; Mathews, F. S.; Goldberg, D. E. Subunit interactions in Ascaris hemoglobin octamer formation. J. Biol. Chem. 1995, 270, 22248-22253.
18. Minning, D.; Goldberg, D. E. Determinants of Ascaris hemoglobin octamer formation. J. Biol. Chem. 1998, 273, 32644-32649.
19. Gibson, Q.; Smith, M. Rates of reaction of Ascaris haemoglobins with ligands. Proc. R. Soc. B 1965, 163, 206-214.
20. Okazaki, T.; Wittenberg, J. B. The hemoglobin of Ascaris perienteric fluid III. Equilibria with oxygen and carbon monoxide. Biochim. Biophys. Acta 1965, 111, 503-511.
21. Parkhurst, L. Hemoglobin and myoglobin ligand kinetics. Annu. Rev. Biophys. 1979, 30, 503-546.
22. Gibson, Q. H.; Began, R.; Olson, J. S.; Carver, T. E.; Dixon, B.; Pohajdak, B.; Sharma, P. K.; Vinogradov, S. N. Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29 to Tyr sperm whale myoglobin mutant. J. Biol. Chem. 1993, 268, 16993-16998.
23. Perutz, M. In The Molecular Basis of Blood Diseases; Stamatoyannopoulis, G., Nienhuis, A. W., Leder, P., Majerus, P. W., Eds.; Saunders: New York, 1987.
24. Carver, T. E.; Brantley, J., R. E.; Singleton, E. W.; Arduini, R. M.; Quillin, M. L.; Phillips, G. N.; Olson, J. S. A novel site-directed mutant of myoglobin with an unusually high oxygen affinity and low autoxidation rate. J. Biol. Chem. 1992, 267, 14443-14450.
25. Kloek, A. P.; Yang, J.; Mathews, F. S.; Frieden, C.; Goldberg, D. E. The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin. J. Biol. Chem. 1994, 269, 2377-2379.
26. DeBaere, I.; Perutz, M. F.; Liger, L.; Marden, M. C.; Poyart, C. Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1994, 97, 1594-1597.
27. Phillips, S. E. V.; Schoenborn, B. P. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature 1981, 292, 81-82.
28. Nagai, K.; Luisi, B.; Shih, D.; Miyazaki, G.; Imai, K.; Poyart, C.; De Young, A.; Kwiatkowsky, L.; Noble, R. W.; Lin, S.-H.; Yu, N.-T. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nature 1987, 329, 858-860.
29. Rohlfs, R. J.; Mathews, A. J.; Carver, T. E.; Olson, J. S.; Springer, B. A.; Egeberg, K. D.; Sligar, S. G. The effect of amino acid substitution at position E7 on the kinetics of ligand binding to sperm whale myoglobin. J. Biol. Chem. 1990, 265, 3168-3176.
30. Huang, S.; Huang, J.; Kloek, A. P.; Goldberg, D. E.; Friedman, J. M. Hydrogen bonding of tyrosine B10 to heme bound oxygen in Ascaris hemoglobin: direct evidence from UV resonance Raman spectroscopy. J. Biol. Chem. 1996, 271, 958-962.
31. Peterson, E.; Huang, S.; Wang, J.; Miller, L.; Vidugiris, G.; Kloek, A.; Goldberg, D.; Chance, M.; Wittenberg, J.; Friedman, J. A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins. Biochemistry 1997, 36, 13110-13121.
32. Xia, Z.; Zhang, W.; Nguyen, B.; La Mar, G.; Kloek, A.; Goldberg, D. 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin. J. Biol. Chem. 1999, in press.
33. Allocatelli, C.; Cutruzzola, F.; Brancaccio, A.; Vallone, B.; Brunori, M. Engineering Ascaris hemoglobin oxygen affinity in sperm whale myoglobin: role of tyrosine B10. FEBS Lett. 1994, 352, 63-66.
34. Zhang, W.; Cutruzzola, F.; Allocatelli, C.; Brunori, M.; La Mar, G. A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: elucidation of the distal hydrogen bonding network by solution NMR. Biophys. J. 1997, 73, 1019-1030.
35. Hamada, K.; Okazaki, T.; Shukuya, R.; Kaziro, K. Hemoglobins from Ascaris lumbricoides. III. A hemoglobin from perienteric fluid. J. Biochem. 1963, 53, 484-488.
36. Hamada, K.; Okazaki, T.; Shukuya, R.; Kaziro, K. Hemoglobins from Ascaris lumbricoides. J. Biochem. 1962, 52, 290-296.
37. Hamada, K.; Okazaki, T.; Shukuya, R.; Kaziro, K. Hemoglobins from Ascaris lumbricoides: reactions of body-wall hemoglobins with ethylisocyanide and potassium cyanide. J. Biochem. 1963, 53, 479-483.
38. Smith, M.; Lee, D. Metabolism of haemoglobin and haematin compounds in Ascaris lumbricoides. Proc. R. Soc. B 1963, 157, 234-257.
39. Okazaki, T.; Wittenberg, B. A.; Briehl, R. W.; Wittenberg, J. B. The hemoglobin of Ascaris body walls. Biochim. Biophys. Acta 1967, 140, 258-265.
40. Blaxter, M.; Vanfleteren, J.; Xia, J.; Moens, L. Structural characterization of an Ascaris myoglobin. J. Biol. Chem. 1994, 269, 30181-30186.
41. Blaxter, M. L. Nemoglobins: Divergent nematode globins. Parasitol. Today 1993, 9, 353-360.
42. Wittenberg, B. A.; Wittenberg, J. B.; Noble, R. W. The reaction of ferrous Ascaris perienteric fluid hemoglobin with hydrogen peroxide. J. Biol. Chem. 1972, 247, 4008-4013.
43. Weber, R. E. Functions of invertebrate hemoglobins with special reference to adaptations to environmental hypoxia. Am. Zool. 1980, 20, 79-101.
44. Riggs, A. F. Aspects of the origin and evolution of nonvertebrate hemoglobins. Am. Zool. 1991, 31, 535-545.
45. Vinogradov, S. N.; Walz, D. A.; Pohajdak, B. Organization of nonvertebrate globin genes. Comp. Biochem. Physiol. 1992, 103B, 759-773.
46. Hardison, R. Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J. Exp. Biol. 1998, 201, 1099-1117.
47. Hardison, R. C. A brief history of hemoglobins: plant, animal, protist, and bacteria. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 5675-5679.
48. Cramm, R.; Siddiqui, R. A.; Friedrich, B. Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus. J. Biol. Chem. 1994, 269, 7349-7354.
49. Crawford, M.; Goldberg, D. Regulation of the Salmonella typhimurium flavohemoglobin gene: a new pathway for bacterial gene expression in response to nitric oxide. J. Biol. Chem. 1998, 273, 34028-34032.
50. Gardner, P.; Gardner, A.; Martin, L.; Salzman, A. Nitric oxide dioxygenase: an enzymatic function for flavohemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 10378-10383.
51. Hausladen, A.; Gow, A.; Stamler, J. Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 14100-14105.
52. LaCelle, M.; Kumano, M.; Kurita, K.; Yamane, K.; Zuber, P.; Nakano, M. Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. J. Bacteriol. 1996, 178, 3803-3808.
53. Membrillo-Hernandez, J.; Coopamah, M.; Channa, A.; Hughes, M.; Poole, R. A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohemoglobin) gene by the NO releaser S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol. Microbiol. 1998, 29, 1101-1112.
54. Poole, R.; Anjum, M.; Membrillo-Hernandez, J.; Kim, S.; Hughes, M.; Stewart, V. Nitric oxide, nitrite, and fnr regulation of hmp (flavohemoglobin) expression in Escherichia coli K-12. J. Bacteriol. 1996, 178, 5487-5492.
55. Crawford, M.; Goldberg, D. Role for the Salmonella flavohemoglobin in protection from nitric oxide. J. Biol. Chem. 1998, 273, 12543-12547.
56. Minning, D.; Gow, A.; Bonaventura, J.; Braun, R.; Dewhirst, M.; Goldberg, D.; Stamler, J. S. Ascaris hemoglobin is a nitric oxide-activated deoxygenase. Nature 1999, 401, 497-502.
57. Jia, L.; Bonaventura, C.; Bonaventura, J.; Stamler, J. S. S-nitrosohemoglobin: a dynamic activity of blood involved in vascular control. Nature 1996, 380, 221-226.
58. Gow, A. W.; Stamler, J. S. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature 1998, 391, 169-173.
59. Sawicki, C. A.; Gibson, Q. H. J. Biol. Chem. 1977, 252, 7538-7547.
60. Bunn, H. F.; Forget, B. G. Hemoglobin: Molecular, Genetic, and Clinical Aspects; Saunders: New York, 1986; Chapter 3.