Cross-linking with O-raffinose lowers oxygen affinity and stabilizes haemoglobin in a non-cooperative T-state conformation

Biochemical Journal

Volumn 384, Issue 2, 2004, Pages 367-375

  Jia, Yiping ^a   Ramasamy, Somasundaram ^b   Wood, Francine ^a   Alayash, Abdu I ^c   Rifkind, Joseph M ^b  

^a CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^b NATIONAL INSTITUTE ON AGING   (United States)

^c NONE

Author keywords

Blood substitute; Haemoglobin; Modified Hb; Oxygen transport; T state

Indexed keywords

CROSSLINKING; DERIVATIVES; HEMOGLOBIN; OXYGEN; PHYSIOLOGY; PROTEINS; REACTION KINETICS;

DEOXYGENATION; OXIDIZED CHAINS; OXYGEN AFFINITY; RAMIFACTIONS;

SUGARS;

2,3 DIPHOSPHOGLYCERIC ACID; DEOXYHEMOGLOBIN; HEMOGLOBIN A; HISTIDINE; NITRITE; RAFFINOSE;

ARTICLE; CHEMICAL REACTION; COMPLEX FORMATION; CONFORMATION; CROSS LINKING; LIGAND BINDING; MOLECULAR DYNAMICS; OXYGEN AFFINITY; OXYGEN TRANSPORT; PH; PRIORITY JOURNAL; REACTION ANALYSIS;

ALLOSTERIC REGULATION; CROSS-LINKING REAGENTS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEMOGLOBIN A, GLYCOSYLATED; HEMOGLOBINS; HUMANS; KINETICS; METHEMOGLOBIN; MOLECULAR CONFORMATION; NITRIC OXIDE; NITRITES; OXYGEN; OXYHEMOGLOBINS; RAFFINOSE; SULFHYDRYL COMPOUNDS;

EID: 10644243494     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040612     Document Type: Article

References (49)

1. Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin. Nature (London) 228, 726-739
2. Perutz, M. F., Wilkinson, A. J., Paoli, M. and Dodson, G. G. (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu. Rev. Biophys. Biomol. Struct. 27, 1-34
3. Johnson, M. B., Adamson, J. G. and Mauk, A. G. (1998) Functional comparison of specifically cross-linked hemoglobins biased toward the R and T states, Biophys. J. 75, 3078-3084
4. Shibayama, N. and Saigo, S. (1995) Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251, 203-209
5. Bettati, S. and Mozzarelli, A. (1997) T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride. J. Biol. Chem. 272, 32050-32055
6. Riess, J. G. (2001) Oxygen carriers ('blood substitutes'): raison d'etre, chemistry, and some physiology. Chem. Rev. 101, 2797-2920
7. 0 and two cross-linked derivatives with hydrogen peroxide: differential behavior of the ferryl intermediate. Arch. Biochem. Biophys. 316, 461-469
8. Baldwin, A. L., Wiley, E. B., Summers, A. G. and Alayash, A. I. (2003) Sodium selenite reduces hemoglobin-induced venulai leakage in the rat mesentery. Am. J. Physiol. Heart Circ. Physiol. 284, H81-H91
9. Adamson, J. G. and Moore, C. (1998) Hemolink™, an O-Raffinose crosslinked hemoglobin-based oxygen carrier. In Blood Substitutes: Principles, Methods, Products and Clinical Trials (Chang, T M. S., ed.), pp. 62-81, Karger Landes Systems, Basel, Switzerland
10. Lieberthal, W., Fuhro, R., Freedman, J. E., Toolan, G., Loscalzo, J. and Valeri, C. R. (1999) O-raffinose cross-linking markedly reduces systemic and renal vasoconstrictor effects of unmodified human hemoglobin, J. Pharmacol. Exp. Ther. 288, 1278-1287
11. Hayashi, A., Suzuki, T. and Shin, M. (1973) An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Biochim. Biophys. Acta 310, 309-316
12. Nagababu, E., Ramasamy, S., Rifkind, J. M., Jia, Y. and Alayash, A. I. (2002) Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry 41, 7407-7415
13. Antonini, E. and Brunori, M. (1971) Hemoglobin and myoglobin in their reactions with ligands. In Frontiers of Biology (Tatum, E. L. and Neuberger, A., eds.), pp. 153-218, North-Holland Publishing Company, Amsterdam
14. Bucci, E. and Fronticelli, C. (1981) Measurement of the Bohr effect: dependence on pH of oxygen affinity of hemoglobin. Methods Enzymol. 76, 523-533
15. Wyman, J. (1948) Heme proteins. Advan. Protein Chem. 4, 407-531
16. Alayash, A. I., Summers, A. G., Wood, F. and Jia, Y. (2001) Effects of giutaraldehyde polymerization on oxygen transport and redox properties of bovine hemoglobin. Arch. Biochem. Biophys. 391, 225-234
17. Doyle, M. L., Lew, G., De Young, A., Kwiatkowski, L., Wierzba, A., Noble, R. W. and Ackers, G. K. (1992) Functional properties of human hemoglobins synthesized from recombinant mutant β-globins. Biochemistry 31, 8629-8639
18. Riddles, P. W., Blakeley, R. L. and Zerner, B. (1983) Reassessment of Ellman's reagent. Methods Enzymol. 91, 49-60
19. Kelman, D. J. and Mason, R. P. (1993) Characterization of the rat hemoglobin thiyl free radical formed upon reaction with phenylhydrazine. Arch. Biochem. Biophys. 306, 439-442
20. Nagababu, E. and Rifkind, J. M. (2002) in Proceedings of the 3rd International Conference on Oxygen/Nitrogen Radicals: Cell Injury and Disease, Morgantown, WV
21. Bellelli, A., Brunori, M., Giardina, B., Condo, S. G., Kothe, N. and Bonhard, K. (1989) Ligand binding to polymerized pyridoxylated hemoglobin. In Blood Substitutes (Chang, T. M. S. and Geyer, R., eds.), pp. 665-666, Marcel Dekker, INC., New York
22. Khan, I., Dantsker, D., Samuni, U., Friedman, A. J., Bonaventura, C., Manjula, B., Acharya, S. A. and Friedman, J. M. (2001) β93 modified hemoglobin: kinetic and conformational consequences. Biochemistry 40, 7581-7592
23. Moore, E. G. and Gibson, Q. H. (1976) Cooperativity in the dissociation of nitric oxide from hemoglobin. J. Biol. Chem. 251, 2788-2794
24. Kon, H. (1975) An interpretation of the three line EPR spectrum of nitric oxide hemeproteins and related model systems: the effect of the heme environment. Biochim. Biophys. Acta 379, 103-113
25. Maxwell, J. C. and Caughey, W. S. (1976) An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds. Biochemistry 15, 388-396
26. Nagai, K., Hori, H., Yoshida, S., Sakamoto, H. and Morimoto, H. (1978) The effect of quaternary structure on the state of the α and β subunits within nitrosyl haemoglobin. Low temperature photodissociation and the ESR spectra. Biochim. Biophys. Acta 532, 17-28
27. Levy, A., Kuppusamy, P. and Rifkind, J. M. (1990) Multiple heme pocket subconformations of methemogiobin associated with distal histidine interactions. Biochemistry 29, 9311-9316
28. Rifkind, J. M., Abugo, O., Levy, A. and Heim, J. (1994) Detection, formation, and relevance of hemichromes and hemochromes. Methods Enzymol. 231, 449-480
29. Doyle, M. P., Picketing, R. A., DeWeert, T. M., Hoekstra, J. W. and Pater, D. (1981) Kinetics and mechanism of the oxidation of human deoxyhemogiobin by nitrites. J. Biol. Chem. 256, 12393-12398
30. Nagababu, E., Ramasamy, S., Abernethy, D. R. and Rifkind, J. M. (2003) Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction. J. Biol. Chem. 278, 46349-46356
31. Bunn, H. F., Wohl, R. C., Bradley, T. B., Cooley, M. and Gibson, Q. H. (1974) Functional properties of hemoglobin Kempsey. J. Biol. Chem. 249, 7402-7409
32. Wajcman, H., Kister, J., Galacteros, F., Spielvogel, A., Lin, M. J., Vidugiris, G. J., Hirsch, R. E., Rriedman, J. M. and Nagel, R. L. (1996) Hb Montefiore (126(H9)Asp → Tyr). High oxygen affinity and loss of cooperativity secondary to C-terminal disruption. J. Biol. Chem. 271, 22990-22998
33. Bonaventura, J. and Riggs, A. (1968) Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. J. Biol. Chem. 243, 980-991
34. Tsai, C. H., Shen, T. J., Ho, N. T. and Ho, C. (1999) Effects of substitutions of lysine and aspartic acid for asparagine at β-108 and of tryptophan for valine at α-96 on the structural and functional properties of human normal adult hemoglobin: roles of α1 β1 and α1 β2 subunit interfaces in the cooperative oxygénation process. Biochemistry 38, 8751-8761
35. O'Donnell, J. K., Birch, P., Parsons, C. T., White, S. P., Okabe, J., Martin, M. J., Adams, C., Sundarapandiyan, K., Manjula, B. N., Acharya, A. S. et al. (1994) Influence of the chemical nature of side chain at β108 of hemoglobin A on the modulation of the oxygen affinity by chloride ions. Low oxygen affinity variants of human hemoglobin expressed in transgenic pigs: hemoglobins Presbyterian and Yoshizuka. J. Biol. Chem. 269, 27692-27699
36. Tsai, C. H. and Ho, C. (2002) Recombinant hemoglobins with low oxygen affinity and high cooperativity. Biophys. Chem. 98, 15-25
37. Imai, K. (1982) Allosteric effects in haemoglobin, Cambridge University press, London
38. Ho, C. and Russu, I. M. (1987) How much do we know about the Bohr effect of hemoglobin? Biochemistry 26, 6299-6305
39. Levy, A., Sharma, V. S., Zhang, L. and Rifkind, J. M. (1992) A new mode for heme-heme interactions in hemoglobin associated with distal perturbations. Biophys. J. 61, 750-755
40. Levy, A. and Rifkind, J. M. (1985) Low-temperature formation of a distal histidine complex in hemoglobin: a probe for heme pocket flexibility. Biochemistry 24, 6050-6054
41. Peisach, J., Blumberg, W. E. and Adler, A. (1973) Electron paramagnetic resonance studies of iron porphin and chlorin systems. Ann. N.Y. Acad. Sci. 206, 310-327
42. Riggs, A. F. (1961) The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium. J. Biol. Chem. 236, 1948-1954
43. Morell, S. A., Huffman, P., Ayeis, V. E. and Taketa, F. (1962) Reversible changes in the NEM-ieactive - SH groups of hemoglobin on oxygenation- deoxygenation. Proc. Natl. Acad. Sci. U.S.A. 48, 1057-1061
44. Benescti, R. E. and Benesch, R. (1962) The influence of oxygenation on the reactivity of the -SH groups of hemoglobin. Biochemistry 1, 735-738
45. Suva, M. M., Rogers, P. H. and Arnone, A. (1992) A third quaternary structure of human hemoglobin A at 1.7 Å resolution. J. Biol. Chem. 267, 17248-17256
46. Monod, J., Wyman, J. and Changeaux, J. P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118
47. Minton, A. P. and Imal, K. (1974) The three-state model: a minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 71, 1418-1421
48. Rivetti, C., Mozzarelli, A., Rossi, G. L., Henry, E. R. and Eaton, W. A. (1993) Oxygen binding by single ctystals of hemoglobin. Biochemistry 32, 2888-2906
49. Niiler, E. (2002) Setbacks for blood substitutes companies. Nature Biotech. 20, 962-963