Negative cooperativity in Root-effect hemoglobins: Role of heterogeneity

Integrative and Comparative Biology

Volumn 47, Issue 4, 2007, Pages 656-661

  Decker, Heinz ^a   Nadja, Hellmann ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; PISCES;

EID: 38749093406     PISSN: 15407063     EISSN: 15577023     Source Type: Journal    
DOI: 10.1093/icb/icm073     Document Type: Article

References (45)

1. Ackers GK, Holt JM. 2006. Asymmetric cooperativity in a symmetric tetramer: human hemoglobin. J Biol Chem 281:11441-3.
2. Ascenzi P, Bocedi A, Fasano M, Gioia M, Marini S, Coletta M. 2005. Proton-linked subunit heterogeneity in ferrous nitrosylated human adult hemoglobin: an EPR study. J Inorg Biochem 99:1255-9.
3. Berenbrink M, Koldkjaer P, Kepp O, Cossins A. 2005. Evolution of oxygen secretion in fishes and the emergence of a complex physiological system. Science 307:1752-7.
4. Binotti I, Giovenco S, Giardina B, Antonini E, Brunori M, Wyman J. 1971. Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood. Arch Biochem Biophys 142:274-80.
5. Brittain T. 2005. Root effect hemoglobins. J Inorg Biochem 99:120-9.
6. Bonaventura C, Godette G, Stevens R, Brenowitz M, Henkens R. 2005. Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin system. J Biol Chem 280:40509-14.
7. Brunori M. 1975. Molecular adaptation to physiological requirements: the hemoglobin system of trout. Curr Top Cell Regul 9:1-39.
8. Brunori M, Coletta M, Giardina B, Wyman J. 1978. A macromolecular transducer as illustrated by trout hemoglobin IV. Proc Natl Acad Sci USA 75:4310-2.
9. Camardella L, Caruso C, D'Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF. 1992. Haemoglobin of the antarctic fish Pagothenia bemacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J Mol Biol 224:449-60.
10. Coletta M, Ascenzi P, D'Avino R, di Prisco G. 1996. Proton-linked subunit kinetic heterogeneity for carbon monoxide binding to hemoglobin from Chelidonichthys kumu. J Biol Chem 271:29859-64.
11. Connelly PR, Robert CH, Briggs WE, Gill SJ. 1986. Analysis of zeros of binding polynomials for tetrameric hemoglobins. Biophys Chem 24:295-309.
12. D'Avino R, Caruso C, Tamburrini M, Romano M, Rutigliano B, Polverino de Laureto P, Camardella L, Carratore V, di Prisco G. 1994. Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. J Biol Chem 269:9675-81.
13. D'Avino R, De Luca R. 2000. Molecular modelling of Trematomus newnesi Hb 1: insights for a lowered oxygen affinity and lack of root effect. Proteins 39:155-65.
14. di Prisco G, Tamburrini M. 1992. The hemoglobins of marine and freshwater fish: the search for correlations with physiological adaptation. Comp Biochem Physiol B 102:661-71.
15. Fago A, Bendixen E, Malte H, Weber RE. 1997. The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a root-effect hemoglobin. J Biol Chem 272:15628-35.
16. Fago A, Carratore V, di Prisco G, Feuerlein RJ, Sottrup-Jensen L, Weber RE. 1995. The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity. J Biol Chem 270:18897-902.
17. Fago A, Romano M, Tamburrini M, Coletta M, D'Avino R, Di Prisco G. 1993. A polymerising root-effect fish hemoglobin with high subunit heterogeneity. Correlation with primary structure. Eur J Biochem 218:829-35.
18. Feuerlein RJ, Weber RE. 1996. Oxygen equilibria of cathodic eel hemoglobin analysed in terms of the MWC model and Adair's successive oxygenation theory. J Comp Physiol B 165:597-606.
19. Henry ER, Bettati S, Hofrichter J, Eaton WA. 2002. A tertiary two-state allosteric model for hemoglobin. Biophys Chem 98:149-64.
20. Imai K, Tsuneshige A, Yonetani T. 2002. Description of hemoglobin oxygenation under universal solution conditions by a global allostery model with a single adjustable parameter. Biophys Chem 98:79-91.
21. Ito N, Komiyama NH, Fermi G. 1995. Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the root effect by comparison of the liganded and unliganded haemoglobin structures. J Mol Biol 250:648-58.
22. Mazzarella L, Bonomi G, Lubrano MC, Merlino A, Riccio A, Vergara A, Vitagliano L, Verde C, di Prisco G. 2006a. Minimal structural requirements for root effect: crystal structure of the cathodic hemoglobin isolated from the antarctic fish Trematomus newnesi. Proteins 62:316-21.
23. Mazzarella L, D'Avino R, di Prisco G, Savino C, Vitagliano L, Moody PC, Zagari A. 1999. Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question. J Mol Biol 287:897-906.
24. Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, di Prisco G. 2006b. High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: the role of histidine residues in modulating the strength of the root effect. Proteins 65:490-8.
25. Mylvaganam SE, Bonaventura C, Bonaventura J, Getzoff ED. 1996. Structural basis for the root effect in haemoglobin. Nat Struct Biol 3:275-83.
26. Olson JS, Rohlfs RJ, Gibson QH. 1987. Ligand recombination to the alpha and beta subunits of human hemoglobin. J Biol Chem 262:12930-8.
27. Pelster B. 2001. The generation of hyperbaric oxygen tensions in fish. News Physiol Sci 16:287-91.
28. Pelster B. 2004. pH regulation and swimbladder function in fish. Respir Physiol Neurobiol 144:179-90.
29. Pelster B, Decker H. 2004. The root effect-a physiological perspective. Micron 35:73-4.
30. Pelster B, Weber RE. 1991. The physiology of the root effect. Adv Comp Environ Physiol 8:51-77.
31. Perutz MF. 1996. Cause of the root effect in fish haemoglobins. Nat Struct Biol 3:211-2.
32. Perutz MF, Brunori M. 1982. Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature 299:421-6.
33. Perutz MF, Mathews FS. 1966. An x-ray study of azide methaemoglobin. J Mol Biol 21:199-202.
34. Root RW. 1931. The respiratory function of the blood of marine fishes. Biol Bull 61:427-56.
35. Tamburrini M, Brancaccio A, Ippoliti R, di Prisco G. 1992. The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Arch Biochem Biophys 292:295-302.
36. Tamburrini M, D'Avino R, Carratore V, Kunzmann A, di Prisco G. 1997. The hemoglobin system of Pleuragramma antarcticum: correlation of hematological and biochemical adaptations with life style. Comp Biochem Physiol A Physiol 118:1037-44.
37. Tamburrini M, Verde C, Olianas A, Giardina B, Corda M, Sanna MT, Fais A, Deiana AM, di Prisco G, Pellegrini M. 2001. The hemoglobin system of the brown moray Gymnothorax unicolor, structure/function relationships. Eur J Biochem 268:4104-11.
38. Tame JR, Wilson JC, Weber RE. 1996. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. J Mol Biol 259:749-60.
39. Tan AL, De Young A, Noble RW. 1972. The pH dependence of the affinity, kinetics, and cooperativity of ligand binding to carp hemoglobin, Cyprinus carpio. J Biol Chem 247:2493-8.
40. Tsuneshige A, Park S, Yonetani T. 2002. Heterotropic effectors control the hemoglobin function by interacting with its T and R states-a new view on the principle of allostery. Biophys Chem 98:49-63.
41. Verde C, Carratore V, Riccio A, Tamburrini M, Parisi E, Di Prisco G. 2002. The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor. J Biol Chem 277:36312-20.
42. Verde C, Parisi E, di Prisco G. 2003. The evolution of polar fish hemoglobin: a phylogenetic analysis of the ancestral amino acid residues linked to the root effect. J Mol Evol 57(Suppl 1):S258-67.
43. Weber RE, Fago A, Val AL, Bang A, Van Hauwaert ML, Dewilde S, Zal F, Moens L. 2000. Isohemoglobin differentiation in the bimodal-breathing amazon catfish Hoplosternum littorale. J Biol Chem 2000;275:17297-305.
44. Yokoyama T, Chong KT, Miyazaki G, Morimoto H, Shih DT, Unzai S, Tame JR, Park SY. 2004. Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect. J Biol Chem 279:28632-10.
45. Yonetani T, Park SI, Tsuneshige A, Imai K, Kanaori K. 2002. Global Slostery model of hemoglobin. Modulation of 0(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J Biol Chem 277:34508-20.