Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Journal of Inorganic Biochemistry

Volumn 100, Issue 9, 2006, Pages 1441-1448

  Juillard, Sandrine ^a   Bondon, Arnaud ^b   Simonneaux, Gérard ^a  

^a UNIVERSITÉ DE RENNES 1   (France)

^b CNRS   (France)

Author keywords

Hemin; Iron porphyrin; Nuclear magnetic resonance; Proton assignment; Reconstituted myoglobin

Indexed keywords

3,7 DIETHYL 2,8 DIMETHYLPORPHYRIN IRON; ALKYL GROUP; APOMYOGLOBIN; FERRIC ION; HEME; HEMIN; HISTIDINE; IMIDAZOLE; IRON COMPLEX; LIGAND; MYOGLOBIN; PROTON; PYRROLE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BOND; CHEMICAL INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; ROTATION; SPECTRUM; SUBSTITUTION REACTION;

ANIMALS; HEME; HORSES; IRON; MAGNETIC RESONANCE SPECTROSCOPY; MAGNETICS; MOLECULAR STRUCTURE; MYOCARDIUM; PORPHYRINS; PROTONS; ROTATION;

EQUUS CABALLUS;

EID: 33747062433     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2006.04.005     Document Type: Article

References (27)

1. Ozaki S., Matsui T., Roach M.P., and Watanabe Y. Coord. Chem. Rev. 198 (2000) 39-59
2. Hayashi T., and Hisaeda Y. Acc. Chem. Res. 35 (2002) 35-43
3. Teale F.W.J. Biochim. Biophys. Acta 35 (1959) 543
4. La Mar G.N., Budd D.L., Viscio D.B., Smith K.M., and Langry K.C. Proc. Natl. Acad. Sci. USA 75 (1978) 5755-5759
5. La Mar G.N., Davis N.L., Parish D.W., and Smith K.M. J. Mol. Biol. 168 (1983) 887-896
6. La Mar G., Toi H., and Krishnamoorthi R. J. Am. Chem. Soc. 106 (1984) 6395-6401
7. Neya S., Fiunasaki N., Sato T., Igarashi N., and Tanaka N. J. Biol. Chem. 268 (1993) 8935-8942
8. Neya S., Funasaki N., Shiro Y., Iizuka T., and Imai K. Biochim. Biophys. Acta 1208 (1994) 31-37
9. Neya S., Funasaki N., and Imai K. J. Biol. Chem. 263 (1988) 8810-8815
10. Neya S., Funasaki N., and Imai K. Biochim. Biophys. Acta 996 (1989) 226-232
11. Tanaka T., Endo A., and Aoyama Y. Bull. Chem. Soc. Jpn. 74 (2001) 907-916
12. Borovkov V.V., Lintuluoto J.M., and Inoue Y. Synlett 1 (1999) 61-62
13. Dawson J.H., Kadkhodayan S., Zhuang C., and Sono M. J. Inorg. Biochem. 45 (1992) 179-192
14. Neya S., and Funasaki N. Biochim. Biophys. Acta 952 (1988) 150-157
15. Neya S., Hori H., Imai K., Kawamura-Konishi Y., Suzuki H., Shiro Y., Iizuka T., and Funasaki N. J. Biochem. 121 (1997) 654-660
16. Antonini E., and Brunori M. Hemoglobin and Myoglobin in Their Reactions with Ligands (1971), North-Holland, Amsterdam
17. Emerson S.D., and La Mar G.N. Biochemistry 29 (1990) 1545-1556
18. La Mar G.N., Budd D.L., and Goff H. Biochem. Biophys. Res. Commun. 77 (1977) 104-110
19. Takahashi S., Lin A.K., and Ho C. Biochemistry 19 (1980) 5196-5202
20. Lecomte J.T.J., and Cocco M.J. Biochemistry 29 (1990) 11057-11067
21. Evans S.V., and Brayer G.D. J. Biol. Chem. 263 (1988) 4263-4268
22. Monzani E., Alzuet G., Casella L., Redaelli C., Bassani C., Sanangelantoni A.M., Gulotti M., De Gioia L., Santagostini L., and Chillemi F. Biochemistry 39 (2000) 9571-9582
23. Levy A., and Rifkind J.M. Biochemistry 24 (1985) 6050-6054
24. Neya S., and Funasaki N. J. Biol. Chem. 262 (1987) 6725-6728
25. Seybert D.W., and Moffat K. J. Mol. Biol. 113 (1977) 419-430
26. La Mar G., Emerson S.D., Lecomte J.T.J., Pande U., Smith K.M., and Kehres L.A. J. Am. Chem. Soc. 108 (1986) 5568-5573
27. La Mar G.N., Pande U., Hauksson J.B., Pandey R.K., and Smith K.M. J. Am. Chem. Soc. 111 (1989) 485-491