The swinging movement of the distal histidine residue and the autoxidation reaction for midge larval hemoglobins

European Journal of Biochemistry

Volumn 270, Issue 7, 2003, Pages 1424-1433

  Kamimura, Satoshi ^a   Matsuoka, Ariki ^b   Imai, Kiyohiro ^c   Shikama, Keiji ^a,d  

^a TOHOKU UNIVERSITY   (Japan)

^b FUKUSHIMA MEDICAL UNIVERSITY   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d PHP Laboratory for Molecular Biology   (Japan)

Author keywords

Distal (E7) histidine; Heme oxidation; Insect (midge) Hb; pH jump; Swinging movement

Indexed keywords

FERRIC ION; HEMOGLOBIN; HEMOPROTEIN; HISTIDINE; LIGAND; METHIONINE; OXYHEMOGLOBIN; WATER;

AMINO ACID TRANSPORT; ARTICLE; AUTOOXIDATION; BOHR EFFECT; FLY; LARVA; MAMMAL; NONHUMAN; OXYGEN AFFINITY; PH; PRIORITY JOURNAL; PROTEIN STABILITY; SPERM;

AMINO ACID SEQUENCE; ANIMALS; CHIRONOMIDAE; CIRCULAR DICHROISM; FLOW INJECTION ANALYSIS; HEMOGLOBINS; HISTIDINE; HYDROGEN-ION CONCENTRATION; INSECT PROTEINS; LARVA; LIGANDS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXYGEN; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRUM ANALYSIS;

ARACHNIDA; CETACEA; CHIRONOMUS THUMMI; HEXAPODA; INSECTA; MAMMALIA; PHYSETER CATODON; TOKUNAGAYUSURIKA AKAMUSI;

EID: 0344406095     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03498.x     Document Type: Article

References (27)

1. Fukuda, M., Takagi, T. & Shikama, K. (1993) Polymorphic hemoglobin from a midge larva (Tokunagayusurika akamusi) can be divided into two different types. Biochim. Biophys. Acta 1157, 185-191.
2. Akiyama, K., Fukuda, M., Kobayashi, N., Matsuoka, A. & Shikama, K. (1994) The pH-dependent swinging-out of the distal histidine residue in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi). Biochim. Biophys. Acta 1208, 306-309.
3. Suzuki, T., Watanabe, Y.-H., Nagasawa, M., Matsuoka, A. & Shikama, K. (2000) Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin: Comparison of the H64 mutants. Eur. J. Biochem. 267, 6166-6174.
4. Riggs, A. (1981) Preparation of vertebrate blood hemoglobins. Methods Enzymol. 76, 14-18.
5. Imai, K. (1981) Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus. Methods Enzymol. 76, 438-449.
6. Shikama, K. & Matsuoka, A. (1989) Spectral properties unique to the myoglobins lacking the usual distal histidine residue. J. Mol. Biol. 209, 489-491.
7. Shikama, K. & Matsuoka, A. (1994) Aplysia myoglobin with unusual properties: Another prototype in myoglobin and haemoglobin biochemistry. Biol. Rev. (Cambridge) 69, 233-251.
8. Matsuoka, A., Kobayashi, N. & Shikama, K. (1992) The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue. Eur. J. Biochem. 210, 337-341.
9. Gotoh, T. & Shikama, K. (1976) Generation of the superoxide radical during autoxidation of oxymyoglobin. J. Biochem. (Tokyo) 80, 397-399.
10. Shikama, K. (1998) The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle. Chem. Rev. 98, 1357-1373.
11. Tsuruga, M., Matsuoka, A., Hachimori, A., Sugawara, Y. & Shikama, K. (1998) The molecular mechanism of autoxidation for human oxyhemoglobin: Tilting of the distal histidine causes nonequivalent oxidation in the β chain. J. Biol. Chem. 273, 8607-8615.
12. Yasuda, J.-P., Ichikawa, T., Tsuruga, M., Matsuoka, A., Sugawara, Y. & Shikama, K. (2002) The α1β1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen: Further evidence from the iron valency hybrids. Eur. J. Biochem. 269, 202-211.
13. Shikama, K. & Matsuoka, A. (1986) Aplysia oxymyoglobin with an unusual stability property: Kinetic analysis of the PH dependence. Biochemistry 25, 3898-3903.
14. Shikama, K. (1988) Stability properties of dioxygen-iron(II) porphyrins: An overview from simple complexes to myoglobin. Coord. Chem. Rev. 83, 73-91.
15. Phillips, S.E.V. & Schoenborn, B.P. (1981) Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature (London) 292, 81-82.
16. Huber, R., Epp, O., Steigemann, W. & Formanek, H. (1971) The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin. Eur. J. Biochem. 19, 42-50.
17. Steigemann, W. & Weber, E. (1979) Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution. J. Mol. Biol. 127, 309-338.
18. Weber, R.E., Braunitzer, G. & Kleinschmidt, T. (1985) Functional multiplicity and structural correlations in the hemoglobin system of larvae of Chironomus thummi thummi (Insect, Diptera): Hb components CTT I, CTT II, CTT III, CTT IV, CTT VI, CTT VIIB, CTT IX and CTT X. Comp. Biochem. Physiol. 80B, 747-753.
19. Di Iori, E.E., Tavernelli, I.W. & Yu, W. (1997) Dynamic properties of monomeric insect erythrocruorin III from Chironomus thummi thummi: Relationships between structural flexibility and functional complexity. Biophys. J. 73, 2742-2751.
20. Hankeln, T., Rozynek, P. & Schmidt, E.R. (1988) The nucleotide sequence and in situ localization of a gene for a dimeric haemoglobin from the midge Chironomus thummi piger. Gene 64, 297-304.
21. Rozynek, P., Hankeln, T. & Schmidt, E.R. (1988) Structure of a hemoglobin gene cluster and nucleotide sequence of three hemoglobin genes from the midge Chironomus thummi piger (Diptera, Insecta). Biol. Chem. Hoppe-Seyler 370, 533-542.
22. Johnson, K.A., Olson, J.S. & Phillips, G.N. Jr (1989) Structure of myoglobin-ethylisocyanide: histidine as a swinging door for ligand entry. J. Mol. Biol. 207, 459-463.
23. Tian, W.D., Sage, J.T. & Champion, P.M. (1993) Investigations of ligand association and dissociation rates in the 'open' and 'closed' states of myoglobin. J. Mol. Biol. 233, 155-166.
24. Springer, B.A., Sligar, S.G., Olson, J.S. & Phillips, G.N. Jr (1994) Mechanisms of ligand recognition in myoglobin. Chem. Rev. 94, 699-714.
25. 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. (1995) A double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobin. J. Biol. Chem. 270, 20763-20774.
26. Brantley, R.E. Jr, Smerdon, S.J., Wilkinson, A.J., Singleton, E.W. & Olson, J.S. (1993) The mechanism of autooxidation of myoglobin. J. Biol. Chem. 268, 6995-7010.
27. Wilps, H. & Zebe, E. (1976) The end-products of anaerobic carbohydrate metabolism in the larvae of Chironomus thummi thummi. J. Comp. Physiol. 112, 263-272.