Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH

Archives of Biochemistry and Biophysics

Volumn 489, Issue 1-2, 2009, Pages 68-75

  Droghetti, Enrica ^a   Sumithran, Suganya ^b   Sono, Masanori ^b   Antalík, Marián ^c   Fedurco, Milan ^d   Dawson, John H ^b   Smulevich, Giulietta ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF SOUTH CAROLINA   (United States)

^c INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^d Michelin Recherche et Technique SA   (Switzerland)

Author keywords

Electronic absorption spectroscopy; Magnetic circular dichroism spectroscopy; Myoglobin; Resonance Raman spectroscopy; Unfolding process; Urea

Indexed keywords

ACETIC ACID; HEME; MYOGLOBIN; UREA;

ACIDITY; ARTICLE; CONTROLLED STUDY; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STRUCTURE;

ACETIC ACID; ANIMALS; CATTLE; HEME; HORSES; HYDROGEN-ION CONCENTRATION; IRON; MOLECULAR STRUCTURE; MYOGLOBIN; PROTEIN DENATURATION; UREA;

EID: 69849090789     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.07.008     Document Type: Article

References (76)

1. Kendrew J.C., Bodo G., Dintzis H., Parrish R., Wyckoff H., and Phillips D. Nature 181 (1958) 662-666
2. Srajer V., Ren Z., Teng T.Y., Schmidt M., Ursby T., Bourgeois D., Pradervand C., Schildkamp W., Wulff M., and Moffat K. Biochemistry 40 (2001) 13802-13815
3. Ostermann A., Waschipky R., Parak F.G., and Nienhaus G.U. Nature 404 (2000) 205-208
4. Schlichting I., and Chu K. Curr. Opin. Struct. Biol. 10 (2000) 744-752
5. Doster W., and Gebhardt R. Chem. Phys. 292 (2003) 383-387
6. Smeller L., Rubens P., and Heremans K. Biochemistry 38 (1999) 3816-3820
7. Meersman F., Smeller L., and Heremans K. Biophys. J. 82 (2002) 2635-2644
8. Fink A.L., Calciano L.J., Goto Y., Kurotsu T., and Palleros D.R. Biochemistry 33 (1994) 12504-12511
9. Goto Y., and Fink A.L. Methods Enzymol. 232 (1994) 3-15
10. Chi Z., and Asher S.A. Biochemistry 38 (1999) 8196-8203
11. Baden N., and Terazima M. J. Phys. Chem. B 110 (2006) 15548-15555
12. Puett D. J. Biol. Chem. 248 (1973) 4623-4634
13. Bismuto E., Colonna G., and Irace G. Biochemistry 22 (1983) 4165-4170
14. Irace G., Bismuto E., Savy F., and Colonna G. Arch. Biochem. Biophys. 244 (1986) 459-469
15. Colonna G., Balestrieri C., Bismuto E., Servillo L., and Irace G. Biochemistry 21 (1982) 212-215
16. Tang Q., Kalsbeck W.A., Olson J.S., and Bocian D.F. Biochemistry 37 (1998) 7047-7056
17. Ramos C.H.I., Kay M.S., and Baldwin R.L. Biochemistry 38 (1999) 9783-9790
18. Muthuselvi L. Chem. Phys. Lett. 465 (2008) 126-130
19. Katz S., and Denis J. Biochim. Biophys. Acta 207 (1970) 331-339
20. Žerovnik E., and Lapanje S. Biophys. Chem. 24 (1986) 53-59
21. Lapanje S., Žerovnik E., and Kranjc Z. Biophys. Chem. 24 (1986) 179-185
22. Pace C.N. Methods Enzymol. 131 (1986) 266-280
23. Harrison S.C., and Blout E.R. J. Biol. Chem. 240 (1965) 299-303
24. Miksovska J., Yom J., Diamond B., and Larsen R.W. Biomacromolecules 7 (2006) 476-482
25. Tofani L., Feis A., Snoke R.E., Berti D., Baglioni P., and Smulevich G. Biophys. J. 87 (2004) 1186-1195
26. Boxer S.G., and Wright K.A. J. Am. Chem. Soc. 101 (1979) 6791-6794
27. Pröll S., Wilhelm B., Robert B., and Scheer H. Biochim. Biophys. Acta 1757 (2006) 750-763
28. Markovic D., Proll S., Bubenzer C., and Scheer H. Biochim. Biophys. Acta 1767 (2007) 897-904
29. Hargrove M.S., and Olson J.S. Biochemistry 35 (1996) 11310-11318
30. Hargrove M.S., Krzywda S., Wilkinson A.J., Dou Y., Ikeda-Saito M., and Olson J.S. Biochemistry 33 (1994) 11767-11775
31. Adams P.A. Biochem. J. 159 (1976) 371-376
32. Lee V.W.S., Chen Y.-L., and Konermann L. Anal. Chem. 71 (1999) 4154-4159
33. Hargrove M.S., Wilkinson A.J., and Olson J.S. Biochemistry 35 (1996) 11300-11309
34. Liong E.C., Dou Y., Scott E.E., Olson J.S., and Phillips G.N. J. Biol. Chem. 276 (2001) 9093-9100
35. Hargrove M.S., Barrick D., and Olson J.S. Biochemistry 35 (1996) 11293-11299
36. Ikeguchi M., Kuwajima K., Mitani M., and Sugai S. Biochemistry 25 (1986) 6965-6972
37. Uversky V.N., and Fink A.L. Biochim. Biophys. Acta 1698 (2004) 131-153
38. Kelly J.W. Curr. Opin. Struct. Biol. 8 (1998) 101-106
39. Rochet J.C., and Lansbury Jr. P.T. Curr. Opin. Struct. Biol. 10 (2000) 60-68
40. Johnson W.G. J. Anat. 196 (2000) 609-616
41. Hoffner G., and Djian P. Biochimie 84 (2002) 273-278
42. Kopito R.R. Trends Cell Biol. 10 (2000) 524-530
43. Noguchi C.T., and Schechter A.N. Annu. Rev. Biophys. Chem. 14 (1985) 239-263
44. Fändrich M., Fletcher M.A., and Dobson C.M. Nature 410 (2001) 165-166
45. Koga T., Taguchi K., Kogiso M., Kobuke Y., Kinoshita T., and Higuchi M. FEBS Lett. 531 (2002) 137-140
46. Eliezer D., Yao J., Dyson H.J., and Wright P.E. Nat. Struct. Biol. 5 (1998) 148-155
47. Bennion B.J., and Daggett V. Proc. Natl. Acad. Sci. USA 100 (2003) 5142-5147
48. J. Almarza, L. Rincon, A.H. Bahsas, F. Brito, Biochemistry, doi:10.1012/bi9007116.
49. Stumpe M.C., and Grubmüller H. J. Am. Chem. Soc. 129 (2007) 16126-16131
50. Stumpe M.C., and Grubmüller H. J. Phys. Chem. B 111 (2007) 6220-6228
51. Caballero-Herrera A., Nordstrand K., Berndt K.D., and Nilsson L. Biophys. J. 89 (2005) 842-857
52. Chow C., Kurt N., Murphy R.M., and Cavagnero S. Biophys. J. 90 (2006) 298-309
53. Vickery L., Nozawa T., and Sauer K. J. Am. Chem. Soc. 98 (1976) 343-350
54. Bracete A.M., Sono M., and Dawson J.H. Biochim. Biophys. Acta 1080 (1991) 264-270
55. Shimizu T., Nozawa T., and Hatano M. Biochim. Biophys. Acta 434 (1976) 126-136
56. Bracete A.M., Kadkhodayan S., Sono M., Huff A.M., Zhuang C., Cooper D.K., Smith K.M., Chang C.K., and Dawson J.H. Inorg. Chem. 33 (1994) 5042-5049
57. Hildebrand D.P., Ferrer J.C., Tang H.L., Smith M., and Mauk A.G. Biochemistry 34 (1995) 11598-11605
58. Pond A.E., Roach M.P., Thomas M.R., Boxer S.G., and Dawson J.H. Inorg. Chem. 39 (2000) 6061-6066
59. Qin J., Perera R., Lovelace L.L., Dawson J.H., and Lebioda L. Biochemistry 45 (2006) 3170-3177
60. Choi S., Spiro T.G., Langry K.C., Smith K.M., Budd D.L., and La Mar G.N. J. Am. Chem. Soc. 104 (1982) 4345-4435
61. Spaulding L.D., Chang C.C., Yu N.-T., and Felton R.H. J. Am. Chem. Soc. 97 (1975) 2517-2525
62. Antonini E., and Brunori M. Hemoglobin and Myoglobin in Their Reactions with Ligands (1971), North-Holland Publishing Co., Amsterdam, the Netherlands
63. Huff A.M., Chang C.K., Cooper D.K., Smith K.M., and Dawson J.H. Inorg. Chem. 32 (1993) 1460-1466
64. Sage J.T., Morikis D., and Champion P.M. Biochemistry 30 (1991) 1227-1237
65. Yang F., and Phillips Jr. G.N. J. Mol. Biol. 256 (1996) 762-774
66. Han S., Rousseau D.L., Giacometti G., and Brunori M. Proc. Natl. Acad. Sci. USA 87 (1990) 205-209
67. Hu S., Smith K.M., and Spiro T. J. Am. Chem. Soc. 118 (1996) 12638-12646
68. Smulevich G., Paoli M., De Sanctis G., Mantini A.R., Ascoli F., and Coletta M. Biochemistry 36 (1997) 640-649
69. Pond A.E., Roach M.P., Sono M., Rux A.H., Franzen S., Hu R., Thomas M.R., Wilks A., Dou Y., Ikeda-Saito M., Ortiz de Montellano P.R., Woodruff W.H., Boxer S.G., and Dawson J.H. Biochemistry 38 (1999) 7601-7608
70. Eaton W.E., and Hochstrasser R.M. J. Chem. Phys. 49 (1968) 985-995
71. Smulevich G., Neri F., Willemsen O., Choudhury K., Marzocchi M.P., and Poulos T.L. Biochemistry 34 (1995) 13485-13490
72. Eakanunkul S., Lukat-Rodgers G.S., Sumithran S., Ghosh A., Rodgers K.R., Dawson J.H., and Wilks A. Biochemistry 44 (2005) 13179-13191
73. Wen N., and Brooker M.H. J. Phys. Chem. 97 (1993) 8608-8616
74. Rasul G., Prakash G.K.S., and Olah G.A. J. Org. Chem. 59 (1994) 2552-2556
75. Hlodan R., Craig S., and Pain R.H. Biotechnol. Genet. Eng. Rev. 9 (1991) 47-88
76. Fink A.L. Fold. Des. 3 (1998) R9-R23