African elephant myoglobin with an unusual autoxidation behavior: Comparison with the H64Q mutant of sperm whale myoglobin

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1387, Issue 1-2, 1998, Pages 165-176

  Tada, Tomoko ^a   Watanabe, Yo Hei ^a   Matsuoka, Ariki ^a   Ikeda Saito, Masao ^b   Imai, Kiyohiro ^c   Ni Hei, Yukio ^a   Shikama, Keiji ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

Author keywords

Elephant, Loxodonta africana; Glutamine (E7) substitution; Myoglobin oxidation; Pentacoordinate form; Sperm whale mutant myoglobin

Indexed keywords

GLUTAMINE; HISTIDINE; MYOGLOBIN;

ABSORPTION SPECTROPHOTOMETRY; AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; AUTOOXIDATION; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ELEPHANT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SKELETAL MUSCLE; SPECIES DIFFERENCE; WHALE;

AFRICA; ANIMALS; ELEPHANTS; HYDROGEN-ION CONCENTRATION; KINETICS; METMYOGLOBIN; MUSCLE, SKELETAL; MYOGLOBIN; OXIDATION-REDUCTION; SPECTROPHOTOMETRY; WHALES;

CETACEA; ELEPHANT; LOXODONTA AFRICANA; PHYSETER CATODON;

EID: 0032497416     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00118-6     Document Type: Article

References (29)

1. Dene H., Goodman M., Romero-Herrera A.E. The amino acid sequence of elephant (Elephas maximus) myoglobin and the phylogeny of Proboscidea. Proc. R. Soc. Lond. B207:1980;111-127.
2. Romero-Herrera A.E., Goodman M., Dene H., Bartnicki D.E., Mizukami H. An exceptional amino acid replacement on the distal side of the iron atom in Proboscidean myoglobin. J. Mol. Evol. 17:1981;140-147.
3. Bartnicki D.E., Mizukami H., Romero-Herrera A.E. Interaction of ligands with the distal glutamine in elephant myoglobin. J. Biol. Chem. 258:1983;1599-1602.
4. Springer B.A., Egeberg K.D., Sligar S.G., Rohlfs R.J., Mathews A.J., Olson J.S. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. J. Biol. Chem. 264:1989;3057-3060.
5. Springer B.A., Sligar S.G., Olson J.S., Phillips G.N. Jr. Mechanisms of ligand recognition in myoglobin. Chem. Rev. 94:1994;699-714.
6. Brantley R.E. Jr., Smerdon S.J., Wilkinson A.J., Singleton E.W., Olson J.S. The mechanism of autooxidation of myoglobin. J. Biol. Chem. 268:1993;6995-7010.
7. Quillin M.L., Arduini R.M., Olson J.S., Phillips G.N. Jr. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234:1993;140-155.
8. Zhao X., Vyas K., Nguyen B.D., Rajarathnam K., La Mar G.N., Li T., Phillips G.N. Jr., Eich R.F., Olson J.S., Ling J., Bocian D.F. A double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobin. J. Biol. Chem. 270:1995;20763-20774.
9. Shikama K., Matsuoka A. Aplysia oxymyoglobin with an unusual stability property: kinetic analysis of the pH dependence. Biochemistry. 25:1986;3898-3903.
10. Shikama K., Matsuoka A. Aplysia myoglobin with unusual properties: another prototype in myoglobin and haemoglobin biochemistry. Biol. Rev. 69:1994;233-251.
11. Shikama K. Stability properties of dioxygen-iron(II) porphyrins: an overview from simple complexes to myoglobin. Coord. Chem. Rev. 83:1988;73-91.
12. Tsubamoto Y., Matsuoka A., Yusa K., Shikama K. Protozoan myoglobin from Paramecium caudatum: its autoxidation reaction and hemichrome formation. Eur. J. Biochem. 193:1990;55-59.
13. Shikama K., Matsuoka A., Iwaasa H. The unique structures of protozoan myoglobin and yeast hemoglobin: an evolutionary diversity. Int. J. Biochem. Cell Biol. 27:1995;1107-1115.
14. Korenaga S., Miki K., Shikama K. A myoglobin-like protein from Tetrahymena pyriformis: isolation and characterization. Eur. J. Protistol. 32:(Suppl. 1):1996;73-78.
15. Bisig D.A., Di Iorio E.E., Diederichs K., Winterhalter K.H., Piontek K. Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin at 1.78-Å resolution. J. Biol. Chem. 270:1995;20754-20762.
16. Rohlfs R.J., Mathews A.J., Carver T.E., Olson J.S., Springer B.A., Egeberg K.D., Sligar S.G. The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin. J. Biol. Chem. 265:1990;3168-3176.
17. De Duve C. A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle. Acta Chem. Scand. 2:1948;264-289.
18. Imai K. Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus. Methods Enzymol. 76:1981;438-449.
19. Shikama K., Matsuoka A. Spectral properties unique to the myoglobins lacking the usual distal histidine residue. J. Mol. Biol. 209:1989;489-491.
20. Gotoh T., Shikama K. Generation of the superoxide radical during autoxidation of oxymyoglobin. J. Biochem. 80:1976;397-399.
21. Satoh Y., Shikama K. Autoxidation of oxymyoglobin: a nucleophilic displacement mechanism. J. Biol. Chem. 256:1981;10272-10275.
22. Shikama K. A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: oxidation, dissociation, or displacement? Biochem. J. 223:1984;279-280.
23. Phillips S.E.V., Schoenborn B.P. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature. 292:1981;81-82.
24. Sugawara Y., Matsuoka A., Kaino A., Shikama K. Role of globin moiety in the autoxidation reaction of oxymyoglobin: effect of 8 M urea. Biophys. J. 69:1995;583-592.
25. T. Tada, The Stability Properties of African Elephant Oxymyoglobin, M.Sci. Thesis, Tohoku University, Sendai, 1994.
26. Matsuoka A., Shikama K. Aplysia oxymyoglobin with an unusual stability property: involvement of two kinds of carboxyl groups. Biochim. Biophys. Acta. 956:1988;127-132.
27. 1H NMR hyperfine shift pattern as a probe for ligation state in high-spin ferric hemoproteins: water binding in metmyoglobin mutants. J. Am. Chem. Soc. 113:1991;7886-7892.
28. Matsuoka A., Kobayashi N., Shikama K. The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue. Eur. J. Biochem. 210:1992;337-341.
29. Ikeda-Saito M., Hori H., Andersson L.A., Prince R.C., Pickering I.J., George G.N., Sanders II C.R., Lutz R.S., McKelvey E.J., Mattera R. Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants. J. Biol. Chem. 267:1992;22843-22852.