Functional characterization of the single hemoglobin of the migratory bird Ciconia ciconia

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 147, Issue 2, 2007, Pages 242-249

  Manconi, Barbara ^a   Olianas, Alessandra ^a   Sanna, Maria T ^a   Messana, Irene ^a   Demurtas, Loredana ^a   Castagnola, Massimo ^b,c   Giardina, Bruno ^b,c   Pellegrini, Mariagiuseppina ^a  

^a UNIVERSITY OF CAGLIARI   (Italy)

^b Istituto di Biochimica   (Italy)

^c CNR   (Italy)

Author keywords

Bohr effect; Chloride; Ciconia ciconia; Enthalpy; Hemoglobin; Migratory bird; Oxygen affinity; Phosphate binding

Indexed keywords

AMINO ACID; CHLORIDE; HEMOGLOBIN; HEMOGLOBIN A; OXYGEN; PHOSPHATE; PHYTIC ACID;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; BIRD; BOHR EFFECT; CICONIA CICONIA; CONTROLLED STUDY; ENTHALPY; HEMOLYSATE; HUMAN; NONHUMAN; OXYGEN AFFINITY; OXYGENATION; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE;

AVES; CICONIA CICONIA;

EID: 34147137117     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.01.017     Document Type: Article

References (56)

1. Abbasi A., and Lutfullah G. Molecular basis of bird respiration: primary hemoglobin structure component from Tufted duck (Aythya fuligula, Anseriformes)-role of α99Arg in formation of a complex salt bridge network. Biochem. Biophys. Res. Commun. 291 (2002) 176-184
2. Amiconi G., Bertollini A., Bellelli A., Coletta M., Condò S.G., and Brunori M. Evidence for two oxygen-linked binding sites for polyanions in dromedary hemoglobin. Eur. J. Biochem. 150 (1985) 387-393
3. Arnone A., and Perutz M.F. Structure of the inositol hexaphospate-human deoxy haemoglobin complex. Nature 249 (1974) 34-36
4. Asakura T., Adachi K., Wiley J.S., Fung L.W., Ho C., Kilmartin J.V., and Perutz M.F. Structure and function of hemoglobin Philly (β35(C1) Tyr → Phe). J. Mol. Biol. 104 (1976) 185-195
5. Braend M., Nesse L.L., and Efremov G.D. Expression and genetics of caprine hemoglobins. Anim. Genet. 18 (1987) 223-231
6. Braunitzer G., and Oberthür W. The primary structure of the hemoglobin of the greylag goose (Anser anser) and the unequal evolution of the β-chains. Hoppe-Seyler Z. Physiol. Chem. 360 (1979) 679-683
7. Brygier J., de Bruin S.H., van Hoof P.M.K.B., and Rollema H.S. The interaction of organic phosphates with human and chicken hemoglobin. Eur. J. Biochem. 60 (1975) 379-383
8. 1 contact. FEBS Lett. 88 (1978) 155-159
9. Corda M., De Rosa M.C., Pellegrini M., Sanna M.T., Olianas A., Fais A., Manca L., Masala B., Zappacosta B., Ficcarra S., Castagnola M., and Giardina B. Adult and fetal haemoglobin J-Sardegna [α50 (CE8) His→Asp]: functional and molecular modelling studies. Biochem. J. 246 (2000) 1193-1199
10. Dickerson R.E., and Geis I. Hemoglobin: Structure, Function, Evolution and Pathology (1983), The Benjamin/Cummings Publishing Co.,Inc., Menlo Park, CA, USA
11. Aγ ratio in fetal hemoglobins. Hemoglobin 5 (1981) 637-651
12. Fermi G., and Perutz M.F. Haemoglobin and myoglobin. In: Phillips D.C., and Richards F.M. (Eds). Atlas of Molecular Structures in Biology, Part 2 (1981), Clarendon Press, Oxford 1-104
13. Giardina B., and Amiconi G. Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures. Methods Enzymol. 76 (1981) 417-427
14. Giardina B., Corda M., Pellegrini M., Condò S.G., and Brunori M. Functional properties of the hemoglobin system of two diving birds (Podiceps nigricollis and Phalacrocorax carbo sinensis). Mol. Physiol. 7 (1985) 281-292
15. Giardina B., Corda M., Pellegrini M.G., Sanna M.T., Brix O., Clementi M.E., and Condò S.G. Flight and heat dissipation in birds: a possible molecular mechanism. FEBS Lett. 270 (1990) 173-176
16. Giardina B., Mosca D., and De Rosa C. The Bohr effect of haemoglobin in vertebrates: an example of molecular adaptation to different physiological requirements. Acta Physiol. Scand. 182 (2004) 229-244
17. A- and β-chains from the only present hemoglobin component. Hoppe-Seyler Z. Physiol. Chem. 365 (1984) 1107-1113
18. Hiebl I., Braunitzer G., and Schneeganss F. The primary structure of the major and minor hemoglobin component of adult Andean goose (Chloephaga melanoptera, Anatidae). The mutation Leu→Ser in position 55 of β-chain. Biol. Chem. Hoppe-Seyler 368 (1987) 1559-1569
19. Hiebl I., Kosters J., and Braunitzer G. High-altitude respiration of birds. The primary structure of the major and minor hemoglobin component of adult goshawk (Accipiter gentilis, Accipitridae). Biol. Chem. Hoppe-Seyler 368 (1987) 333-342
20. Hiebl I., Schneeganss D., Grimm F., Kosters J., and Braunitzer G. High altitude respiration of bird: the primary structure of the major and minor hemoglobin component of adult European black vulture (Aegypius monachus, Aegypiinae). Biol. Chem. Hoppe-Seyler 368 (1987) 11-18
21. Hiebl I., Weber R.E., Schneeganss D., Kosters J., and Braunitzer G. High altitude respiration in birds: structural adaptations in the major and minor hemoglobin component of adult Ruppell's griffon (Gyps rueppellii, Aegypiinae). A new molecular pattern for hypoxic tolerance. Biol. Chem. Hoppe-Seyler 369 (1988) 217-232
22. Hiebl I., Weber R.E., Schneeganss D., and Braunitzer G. High-altitude respiration in Falconiformes: the primary structure and functional properties of the major and minor hemoglobin component of adult white headed vulture (Trigonoceps occipitalis, Aegypiinae). Biol. Chem. Hoppe-Seyler 370 (1989) 699-706
23. Huber K., Braunitzer G., Schneeganss D., Kosters J., and Grimm F. The primary structure of the hemoglobin of the cormorant (Phalacrocorax carbo, Pelecaniformes). Biol. Chem. Hoppe-Seyler 369 (1988) 1251-1258
24. D-globin gene. Biochem. Biophys. Res. Commun. 234 (1997) 450-453
25. Isaacks R., Harkness D.R., Sampsell R., Adler J.L., Roth S., Kim C.Y., and Goldman P.H. Studies on avian erythrocyte metabolism. Inositol tetrakisphosphate: the major phosphate compound in the erythrocytes of the ostrich (Struthio camelus camelus). Eur. J. Biochem. 77 (1977) 567-574
26. Isaacks R., Harkness D.R., Goldman P.H., Adler J.L., and Kim C.Y. Studies on the avian erythrocyte metabolism. VII. Effect of inositol pentaphosphate and other organic phosphates on oxygen affinity of the embryonic and adult-type hemoglobins of the turkey embryo. Hemoglobin 1 (1977) 577-593
27. Jessen T.H., Weber R.E., Fermi G., Tame J., and Braunitzer G. Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 6519-6522
28. Knapp J.E., Oliveira M.A., Xie Q., Ernst S.R., Riggs A.F., and Hackert M.L. The structural and functional analysis of the hemoglobin D component from chicken. J. Biol. Chem. 274 (1999) 6411-6420
29. Ladner R.C., Heidner E.J., and Perutz M.F. The structure of horse methaemoglobin at 2.0 Å resolution. J. Mol. Biol. 114 (1977) 385-414
30. Lange D., and Hild J. Leipzig/Halle Airport. A presentation. Bird Aviat. 23 (2003) 1-8
31. Liang Y., Hua Z., Liang X., Xu Q., and Lu G. The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity. J. Mol. Biol. 313 (2001) 123-137
32. Manca L., Formato M., Demuro P., Gallisai D., Orzalesi M., and Masala B. The γ globin chain heterogeneity of the Sardinian newborn baby. Hemoglobin 10 (1986) 519-528
33. Manca L., De Muro P., and Masala B. Hb G-Philadelphia, or [α68(E17)Asn→Lys], in North Sardinia: detection by isoelectric focusing and HPLC of tryptic peptides. Clin. Chim. Acta 177 (1988) 231-238
34. Aγ (E19)Ile→Tyr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes. Clin. Chim. Acta 198 (1991) 195-202
35. Mejia O., Leon-Velarde F., and Monge C. The effect of inositol hexaphosphate in the high-affinity haemoglobin of the Andean chicken (Gallus gallus). Comp. Biochem. Physiol. B 109 (1994) 437-441
36. Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., and Johnson M.H. Hemoglobin Presbyterian: β108 (G10) Asn→Lys, a hemoglobin variant with low oxygen affinity. FEBS Lett. 92 (1978) 53-56
37. Oberthür W., Braunitzer G., Baumann R., and Wright P. Die primarstruktur der α- und β-ketten der hauptkomponenten der hamoglobine der strobes (Struthio camelus) und des nandus (Rhea americana) (Struthio formes). Aspekte zur alungs physiologie und systematic. Hoppe-Seyler Z. Physiol. Chem. 363 (1983) 119-134
38. O'Donnell S., Mandaro R., Schuster T.M., and Arnone A. X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for a location of a proton- and oxygen-linked chloride binding site at valine 1α. J. Biol. Chem. 254 (1979) 12204-12208
39. Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 228 (1970) 726-734
40. Perutz M.F. The Bohr effect and combination with organic phosphates. Nature 228 (1970) 734-739
41. Perutz M.F. Species adaptation in a protein molecule. Mol. Biol. Evol. 1 (1983) 1-28
42. Perutz M.F. Mechanism of cooperativity and allosteric regulation. Q. Rev. Biophys. 22 (1989) 139-236
43. Rollema H.S., and Bauer C. The interaction of inositol pentaphospate with the hemoglobin of highland and lowland geese. J. Biol. Chem. 254 (1979) 12038-12043
44. Schnek A.G., Paul C., and Léonis J. Evolution and adaptation of avian and crocodilian hemoglobins. In: Lamy J., Truchot J.-P., and Gilles R. (Eds). Respiratory Pigments in Animals. Relation Structure-Function (1985), Springer-Verlag, Heidelberg 141-158
45. Shih D.T., Luisi B.F., Miyazaki G., Perutz M.F., and Nagai K. A mutagenic study of the allosteric linkage of His(HC3)146β in haemoglobin. J. Mol. Biol. 230 (1993) 1291-1296
46. Tamburrini M., Condò S.G., di Prisco G., and Giardina B. Adaptation to extreme environments: structure-function relationship in emperor penguin hemoglobin. J. Mol. Biol. 237 (1994) 615-621
47. Tomita S., and Riggs A. Studies of the interaction of 2,3-diphophoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant. J. Biol. Chem. 246 (1971) 547-554
48. Van Beek G.G., and De Bruin S.H. Identification of the residues involved in the oxygen-linked chloride-ion binding sites in human deoxyhemoglobin and oxyhemoglobin. Eur. J. Biochem. 105 (1980) 353-360
49. Vandecasserie C., Paul C., Schnek A.G., and Léonis J. Oxygen affinity of avian hemoglobins. Comp. Biochem. Physiol. A 44 (1973) 711-718
50. Wang H.C., Liang Y.H., Zhu J.P., and Lu G.Y. Crystallization and preliminary studies of bar-headed goose fluoromethaemoglobin with inositol hexaphosphate. Acta Crystallogr., D Biol. Crystallogr. 56 (2000) 1183-1184
51. Weber R.E. Molecular strategies in the adaptation of vertebrate hemoglobin function. In: Wood S.C., Weber R.E., Hargens A.R., and Millard R.W. (Eds). Physiological Adaptation in Vertebrates. Respiration, Circulation and Metabolism (1992), Dekker, M., Inc., New York
52. Weber R.E., Hiebl I., and Braunitzer G. High altitude and hemoglobin function in the vultures Gyps rueppellii and Aegypius monachus. Biol. Chem. Hoppe-Seyler 369 (1988) 233-240
53. 55-Ser): functions related to high-altitude respiration in geese. J. Appl. Physiol. 75 (1993) 2646-2655
54. Winslow R.M., and Anderson W.F. The hemoglobinopathies. In: Stambury J.B., Wyngaardeen J.B., and Fredrickson D.S. (Eds). The Metabolic Basis of Inherited Disease. 4th edn. (1978), McGraw-Hill, Inc., New York, USA 1465-1507 Part 10
55. Yasuda J.P., Ichikawa T., Tsuruga M., Sugawara Y., Shikama K., and Matsuoka A. The alpha 1 beta 1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen. Eur. J. Biochem. 269 (2002) 202-211
56. Zhang J., Hua Z., Tame J.R., Lu G., Zhang R., and Gu X. The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form). J. Mol. Biol. 26 255 (1996) 484-493