Extreme pH sensitivity in the binding of oxygen to some fish hemoglobins. the root effect

The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins

Volumn , Issue , 2008, Pages 219-234

  Brittain, T ^a  

^a UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 44749091800     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-044452839-1.50010-3     Document Type: Chapter

References (76)

1. Root R.W. Biol. Bull. Mar. Biol. Lab. Woods Hole. 1931, 61:427-456.
2. Dickerson R.E. J. Mol. Evol. 1971, 1:26-45.
3. Dickerson R.E., Geiss I. Hemoglobin: Structure, Function, Evolution and Pathology 1983, Benjamin Cummings, U.S.A.
4. Lukin J.A., Simplaceanu V., Zou M., et al. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:10345-10358.
5. Colman J.P., Brauman J.I., Iverson B.L., et al. J. Amer. Chem. Soc. 1983, 105:3052-3056.
6. Olson J.S., Mathews A.J., Rohlfs R.J., et al. Nature 1988, 336:256-266.
7. Slebodnick C., Ibers J.A. J. Bio. Inorg. Chem. 1997, 2:521-525.
8. Olson J.S., Phillips G.N. J. Bio. Inorg. Chem. 1997, 2:544-552.
9. Sigfridson E., Ryde U. J. Bio. Inorg. Chem. 1999, 4:99-110.
10. Nagai K., Pertuz M.F., Poyart C. Proc. Natl. Acad. Sci. U.S.A. 1985, 82:7252-7255.
11. Perutz M.F. Nature 1970, 228:726-739.
12. Perutz M.F. Mechanisms of Cooperativity and Allosteric Regulation in Proteins 1990, Cambridge University Press, Cambridge, U.K.
13. Monod J., Wyman J., Changeaux J.P. J. Mol. Biol. 1965, 12:88-118.
14. Koshland D.E., Nemethy G., Filmer D. Biochem. 1966, 5:365-385.
15. Szabo A., Karplus M. J. Mol. Biol. 1972, 72:163-197.
16. Benesch R., Benesch R.E. Biochem. Biophys. Res. Com. 1967, 26:162-167.
17. Imaizumi K., Imai K., Tyuma I. J. Biochem. (Tokyo) 1979, 86:1829-1840.
18. Kilmartin J.V., Rossi-Bernardi L. Physiol. Rev. 1973, 53:836-890.
19. Pertuz M.F., Muirhead H., Mazzarella L., et al. Nature 1969, 222:1240-1243.
20. Perutz M.F., Kilmartin J.V., Nishikura K., et al. J. Mol. Biol. 1980, 138:649-670.
21. Perutz M.F., Pulsinella P.D., Ten L., et al. J. Mol. Biol. 1980, 138:648-660.
22. Perutz M.F., Pulsinella P.D., Ten L., et al. Nature 1971, 232:147-149.
23. Kilmartin J.V., Hewitt J.A., Wooton J.F. J. Mol. Biol. 1975, 93:203-218.
24. Shih D.T.B., Luisi B.F., Miyazaki G., et al. J. Mol. Biol. 1993, 230:1291-1296.
25. Perutz M.F., Fermi G., Shih D.T.B. Proc. Natl. Acad. Sci. U.S.A. 1984, 81:4781-4785.
26. Kilmartin J.V., Breen J.J., Roberts G.C.K. Proc. Natl. Acad. Sci. U.S.A. 1973, 70:1246-1249.
27. Kilmartin J.V., Wooton J.F. Nature 1970, 228:766-767.
28. Kilmartin J.V., Rossi-Bernardi L. Nature 1969, 222:1243-1246.
29. Nishikura K. Biochem. J. 1978, 173:651-657.
30. Russu I.M., Ho N.T., Ho C. Biochemistry 1980, 19:1043-1052.
31. Mathews J.B., Hanania G.F.H., Gurd F.R.N. Biochemistry 1979, 18:1928-1936.
32. Minton A.P., Imai K. Proc. Natl. Acad. Sci. U.S.A. 1974, 71:1418-1421.
33. Smith F.R., Lattman E.E., Carter C.W. Proteins. 1991, 10:81-91.
34. Silva M.M., Rogers P.H., Arnone A. J. Biol. Chem. 1992, 267:17248-17256.
35. Janin J., Wodack S.J. Proteins 1993, 15:1-4.
36. Srinivasen R., Rose G.D. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:11113-11117.
37. Bettati E.R.S., Hofrichter J., Eaton W.A. Biophys. Chem. 2002, 98:149-164.
38. Shibayama N., Muira S., Tame J.R.H., et al. J. Biol. Chem. 2002, 277:38791-38796.
39. Yonetani T., Park S., Tsuneshige A., et al. J. Biol. Chem. 2002, 277:34508-34520.
40. Tsuneshige A., Park S., Yonetani T. Biophys. Chem. 2002, 98:49-63.
41. Imai K., Tsuneshige A., Yonetani T. Biophys. Chem. 2002, 98:79-91.
42. Root R.W., Irving L. Biol. Bull. Mar. Biol. Lab. Woods Hole. 1943, 84:207-212.
43. Root R.W., Irving L. Biol. Bull. Mar. Biol. Lab. Woods Hole 1941, 81:307-323.
44. Green A.A., Root R.W. Biol. Bull. Mar. Biol. Lab. Woods Hole 1933, 64:383-404.
45. Brittain T. Comp. Biochem. Physiol. 1987, 86:473-481.
46. Brittain T. Comp. Biochem. Physiol. 1986, 85:241-243.
47. Brittain T. Biochem. J. 1985, 228:409-414.
48. Binotti I., Giovenco S., Giardina B., et al. Arch. Biochem. Biophys. 1971, 142:274-280.
49. Brunori M., Falconi G., Fortuna G., Giardina B. Arch. Biochem. Biophys. 1975, 168:512-519.
50. Ingerman R.L., Terwilliger R.C. J. Exp. Biol. 1982, 220:171-177.
51. Waser W.P., Heisler N. Fish Physiol. Biochem. 2004, 30:77-85.
52. Scholander V.V.P., van Dam L. Biol. Bull. Mar. Biol. Lab. Woods Hole. 1954, 107:247-259.
53. Pelster B. News Physiol. Sci. 2001, 16:287-291.
54. Berenbrink M., Koldkjaer P., Kepp O., Cossins A.R. Science 2005, 307:1752-1757.
55. Pelster B., Decker H. Micron. 2004, 35:73-74.
56. Bonaventura C., Crumbliss A.L., Weber R.E. Acta. Physiol. Scand. 2004, 182:245-258.
57. Noble R.W., Parkhurst L.J., Gibson Q.H. J. Biol. Chem. 1970, 245:6628-6633.
58. Tan A.L., De Young A., Noble R.W. J. Biol. Chem. 1972, 247:2493-2498.
59. Tan A.L., Noble R.W., Gibson Q.H. J. Biol. Chem. 1973, 248:2880-2888.
60. Pennelly R.R., Tan-Wilson A.L., Noble R.W. J. Biol. Chem. 1975, 250:7239-7244.
61. Wyman J., Gill S.J., Gaud H.T., et al. J. Mol. Biol. 1978, 124:161-175.
62. Brunori M., Coletta M., Giardina B., Wyman J. Proc. Natl. Acad. Sci. U.S.A. 1978, 75:4310-4312.
63. Parkhurst L.J., Goss D.J., Perutz M.F. Biochem. 1983, 22:5401-5409.
64. Perutz M.F., Brunori M. Nature 1982, 299:421-426.
65. Bossa F., Barra D., Petruzelli R., et al. Biochim. Biophys. Acta 1978, 536:298-305.
66. Luisi B.F., Nagai K. Nature 1986, 320:555-556.
67. Ito N., Komiyama N.H., Fermi G. J. Mol. Biol. 1995, 250:648-658.
68. Camardella L., Caruso C., D'Avino R., et al. J. Mol. Biol. 1992, 224:449-460.
69. Verde C., Parisi E., di Prisco G. J. Mol. Evol. 2003, 57:5258-5267.
70. Yokoyama T., Chong K.T., Miyazaki G., et al. J. Biol. Chem. 2004, 279:28632-28640.
71. Perutz M.F. Nat. Struct. Biol. 1996, 3:211-212.
72. Mylvaganam S.E., Bonaventura C., Bonaventura J., Getzoff E.D. Nat. Struct. Biol. 1996, 3:275-283.
73. Luisi B.F., Nagai K., Perutz M.F. Acta Haemat. 1987, 78:85-89.
74. Mazzarella L., D'Avino R., Di Prisco G., et al. J. Mol. Biol. 1999, 287:897-906.
75. D'Avino R., DeLuca R. Proteins 2000, 39:155-165.
76. Hill A.V. J. Physiol. (London) 1910, 40:4-7.