Structures of a hemoglobin-based blood substitute: Insights into the function of allosteric proteins

Structure

Volumn 5, Issue 2, 1997, Pages 227-237

  Kroeger, Kenneth S ^a   Kundrot, Craig E ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

allostery; blood substitutes; hemoglobins; molecular structure

Indexed keywords

EID: 0031568811     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00181-0     Document Type: Article

References (57)

1. Kumar, R. (1995). Recombinant hemoglobins as blood substitutes: a biotechnology perspective. Proc. Soc. Exp. Biol. Med. 208, 150-158.
2. Pool, R. (1990). Slow going for blood substitutes. Science 250, 1655-1656.
3. Zuck, T.F. & Riess, J.G. (1994). Current status of injectable oxygen carriers. Crit. Rev. Clin. Lab. Sci. 31, 295-324.
4. Benesch, R. & Benesch, R.E. (1967). The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Commun. 26, 162-167.
5. Bunn, H.F., Esham, W.T. & Bull, R.W. (1969). The renal handling of hemoglobin. I. glomerular filtration. J. Exp. Med. 129, 909-923.
6. Bunn, H.F. & Jandl, J.H. (1969). The renal handling of hemoglobin. II. catabolism. J. Exp. Med. 129, 925-934.
7. Looker, D.,et al., & Fermi, G. (1992). A human recombinant haemoglobin designed for use as a blood substitute. Nature 356, 258-260.
8. Moo-Penn, W.F., Wolff, J.A., Simon, G., Vacek, M., Jue, D.L., & Johnson, M.H. (1978). Hemoglobin Presbyterian: β108 (G10) asparagine• lysine. A hemoglobin variant with low oxygen affinity. FEBS Lett. 92, 53-56.
9. Lesson, R., et al., & Loveday, M. (1996). A safety study of recombinant human hemoglobin for intraoperative transfusion therapy. Anesth. Analg. 82, 5275.
10. Fermi, G., Perutz, M.F., Shaanan, B. & Fourme, R. (1984). The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175, 159-174.
11. Shaanan, B. (1983). Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171, 31-59.
12. Smith, F.R., Lattman, E.E. & Carter, C.W.J. (1991). The mutation β99 Asp-Tyr stabilizes Y-A new, composite quaternary state of human hemoglobin. Proteins 10, 81-91.
13. Silva, M.M., Rogers, P.M. & Arnone, A. (1992). A third quaternary structure of human hemoglobin A at 1.7 Å resolution. J. Biol. Chem. 267, 17248-17256.
14. Baldwin, J. & Chothia, C. (1979). Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129, 175-220.
15. Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118.
16. Antonini, E. & Brunori, M. (1971). Hemoglobin and myoglobin in their reaction with ligands. American Elsevier Publishing Co., Inc., NY, USA.
17. Ward, K.B., Wishner, B.C., Lattman, E.E. & Love, W.E. (1975). Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions. J. Mol. Biol. 98, 161-177.
18. Baldwin, J.M. (1980). The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution. J. Mol. Biol. 136, 103-128.
19. Ladner, R.C., Heidner, E.J. & Perutz, M.F. (1977). The structure of horse methaemoglobin at 2.0 Å resolution. J. Mol. Biol. 114, 385-414.
20. Smith, F.R. & Simmons, K.C. (1994). Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure. Proteins 18, 295-300.
21. Janin, J. & Wodak S.J. (1993). The quaternary structure of carbonmonoxy hemoglobin Ypsilanti. Proteins 15, 1-4.
22. Srinivasan, R. & Rose, G.D. (1994). The T-to-R transformation in hemoglobin: a re-evaluation. Proc. Natl. Acad. Sci. USA 91, 11113-11117.
23. Nishikawa, K., Ooi, T., Ysogai, Y & Saito, N. (1972). Tertiary structure of Proteins. I. Representation and computation of the conformations. J. Phys. Soc. Jpn. 32, 1331-1337.
24. Richards, F.M. & Kundrot, C.E. (1988). Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure. Proteins 3, 71-84.
25. Kavanaugh, J.S., Rogers, P.H. & Arnone, A. (1992). High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from β-globins having mutated amino termini. Biochemistry 31, 8640-8647.
26. Bisig, D.A., Di lorio, E.E., Diederichs, K., Winterhalter, K.H. & Piontek, K. (1995). Crystal structure of Asian Elephant (Elephas maximus) cyano-metmyoglobin at 1.78 Å resolution. J. Biol. Chem. 270, 20754-20762.
27. Conti, E., et al., & Bolegnesi, M. (1993). X-ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states. J. Mol. Biol. 233, 498-508.
28. Evans, S.V., Sishta, B.P., Mauk, A.G. & Brayer, G.D. (1994). Three-dimensional structure of cyanomet-sulfmyoglobin C. Proc. Natl. Acad. Sci. USA 91, 4723-4726.
29. Honzatko, R.B., Hendrickson, WA. & Love, W.E. (1985). Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus. J. Mol. Biol. 184, 147-164.
30. Steigemann, W. & Weber, E. (1979). Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution. J. Mol. Biol. 127, 309-338.
31. Kolatkar, P.R., Ernst, S.R. & Hackert M.L. (1992). Structure determination and refinement of homotetrameric hemoglobin from Urechis caupo at 2.5 Å resolution. Acta Cryst. B 48, 191-199.
32. Mitchell, D.T., Kitto, G.B. & Hackert, M.L. (1995). Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola. J. Mol. Biol. 251, 421-431.
33. Neya, S., Funasaki, N., Sato, T., Igarashi, N. & Tanaka, N. (1993). Structural analysis of the myoglobin reconstituted with iron porphine. J. Biol. Chem. 268, 8935-8942.
34. Tyuma, I. (1966). The preparation and properties of the isolated alpha and beta subunits of hemoglobin A. Biochemistry 5, 2957-2962.
35. Brunori, M., Noble, R.W., Antonini, E. & Wyman, J. (1966). The reactions of the isolated alpha and beta chains of human hemoglobin with oxygen and carbon monoxide. J. Biol. Chem. 241, 5238-5243.
36. Pauling, L. (1935). The oxygen equilibrium of hemoglobin and its structural interpretation. Proc. Natl. Acad. Sci. USA 21, 186-191.
37. Wyman, J. (1948). Heme proteins. Adv. Protein Chem. 4, 407.
38. Koshland, D.E.J., Némethy, G. & Filmer, D. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-385.
39. Szabo, A. & Karplus, M. (1972). A mathematical model for structure-function relations in hemoglobin. J. Mol. Biol. 72, 163-197.
40. Herzfeld, J. & Stanley, H.E. (1974). A general approach to cooperativity and its application to the oxygen equilibrium of hemoglobin and its effectors. J. Mol. Biol. 82, 231-265.
41. Johnson, M.L., Turner, B.W. & Ackers, G.K. (1984). A quantitative model for the cooperative mechanism of human hemoglobin. Proc. Natl. Acad. Sci. USA 81, 1093-1097.
42. Di Cera, E., Robert, C.H. & Gill, S.J. (1987). Allosteric interpretation of the oxygen-binding reaction of human hemoglobin tetramers. Biochemistry 26, 4003-4008.
43. Doyle, M.L. & Ackers, G.K. (1992). Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Biochemistry 31, 11182-11195.
44. Di Cera, E. (1995). Thermodynamic theory of site-specific binding processes in biological macromolecules. Cambridge University Press, NY, USA.
45. Perutz, M.F., Muirhead, H., Cox, J.M. & Goaman, L.C. (1968). Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: the atomic model. Nature 219, 131-139.
46. Ho, C. (1992). Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 43, 153-312.
47. Doyle, M.L., et al., & Ackers G. K. (1992). Functional properties of human hemoglobins synthesized from recombinant mutant beta-globins. Biochemistry 31, 8629-8639.
48. Perutz, M.F. & Imai, K. (1980). Regulation of oxygen affinity of mammalian hemoglobins. J. Mol. Biol. 136, 183-191.
49. Arnone, A., Benesch, R.E. & Benesch, R. (1977). Structure of human deoxyhemoglobin specifically modified with pyridoxal compounds. J. Mol. Biol. 115, 627-642.
50. Russu, I.M., Ho, N.T. & Ho, C. (1987). A proton nuclear Overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin. Biochim Biophys Acta 914, 40-48.
51. Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21, 916-924.
52. Kabsch, W. (1988). Automatic indexing of rotation diffraction patterns. J. Appl. Cryst. 21, 67-71.
53. Blum, M., Metcalf, P., Harrison, S.C. & Wiley, D.C. (1987). A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector. J. Appl. Cryst. 20, 235-242.
54. Brünger, A.T. (1992). X-PLOR Version 3.1. A system for X-ray crystallography and NMR. Yale University Press, New Haven, CT, USA.
55. Jones, T.A., Zou, Y.-Y. & Cowan, S.W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
56. Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
57. Lee, B. & Richards, F.M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.