Structural basis for the root effect in haemoglobin

Nature Structural Biology

Volumn 3, Issue 3, 1996, Pages 275-283

  Mylvaganam, Shankari E ^a   Bonaventura, Celia ^b   Bonaventura, Joseph ^b   Getzoff, Elizabeth D ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b DUKE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN;

ADAPTATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BOHR EFFECT; CRYSTAL STRUCTURE; FISH; NONHUMAN; OXYGENATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; SWIMMING; TELEOST; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; ELECTROCHEMISTRY; FISHES; HEMOGLOBINS; HUMANS; HYDROGEN-ION CONCENTRATION; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

EID: 0029927657     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0396-275     Document Type: Article

References (17)

1. Root, R.W. The respiratory function of the blood of marine fishes. Biol. Bull. 61, 427-465 (1931).
2. Brunori, M., Coletta, M., Giardina, B. & Wyman, J. A macromolecular transducer as illustrated by trout haemoglobin IV. Proc. Natl. Acad. Sci. USA 75, 4310-4312 (1978).
3. Steen, J.B. in Fish Physiology 4th edn. (eds Hoar, W.S. & Randall, D.J.) 413-443 (Academic Press, New York. 1970).
4. Farmer, M., Fyhn, HJ., Fyhn, U.E.H. & Noble, R.W. Occurrence of Root effect haemoglobins in Amazonian fishes. Comp. Biochem. Physiol. 62A, 115-124 (1979).
5. Wittenberg, J.B. & Wittenberg, B.A. The choroid rete mirabile of the fish eye. I. oxygen secretion and structure: comparison with the swimbladder rete mirabile. Biol. Bull. 146, 116-136 (1974).
6. Brittain, T. Minireview. The Root effect. Comp. Biochem. Physiol. 86B, 473-481 (1987).
7. Riggs, A. Studies of the Amazonian fishes: an overview. Comp. Biochem. Physiol. 62A, 257-272 (1979).
8. diPrisco, G. & Tamburrini, M. The hemoglobins of marine and freshwater fish: the search for correlations with physiological adaptation. Comp. Biochem. Physiol. 102B, 661-671 (1992).
9. Bohr, C., Hasselbalch, K., & Krogh, A. Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt. Skand. Arch. Physiol. 16, 402-412 (1904).
10. Perutz, M.F. & Brunori, M. Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature 299, 421-426 (1982).
11. Tan, A.L., De Young, A. & Noble, R. W. The pH dependence of the affinity, kinetics, and cooperativity of ligand binding to carp haemoglobin, Cyprinus carpio. J. Biol. Chem. 247, 2493-2498 (1972).
12. Noble, R.W., Parkhurst, U. & Gibson, Q.H. The effect of pH on the reactions of oxygen and carbon monoxide with the haemoglobin of the carp, Cyprinus carpio. J. Biol. Chem. 245, 6628-6633 (1970).
13. Scholander, P.F. & Van Dam, L. Secretion of gases against high pressure in the swim-bladder of deep sea fishes. I. Oxygen dissociation in blood. Biol. Bull. 107, 247-259 (1954).
14. Bonaventura, C., Boiling, S. Bonaventura, J., & Brunori, M. Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost. J. Biol. Chem. 251, 1871-1876 (1976).
15. Horimoto, K., Suzuki, H. & Otsuka, J. Discrimination between adaptive and neutral amino acid substitutions in vertebrate haemoglobins. J. Molec. Evol. 31, 302-324 (1990).
16. Parkhurst, L.J., Goss, D.J. & Perutz, M.F. Kinetic and equilibrium studies on the role of β-147 histidine in the Root effect and cooperativity in carp hemoglobin. Biochemistry 22, 5401-5409 (1983).
17. Parkurst, L.J. & Goss, D.J. Ligand binding kinetic studies on the hybrid hemoglobin α(human):β(carp): a hemoglobin with mixed conformations and sequential conformationsl changes. Biochemistry 23, 2180-2186 (1984).