Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: An ITC study

Biophysical Chemistry

Volumn 90, Issue 3, 2001, Pages 279-299

  Hellmann, N ^a   Jaenicke, E ^a   Decker, H ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Allosteric interaction; Cooperativity; Hemocyanin; Isothermal titration calorimetry; Nesting model; Urate

Indexed keywords

CAFFEINE; HEMOCYANIN; OXYGEN; URATE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALORIMETRY; CONTROLLED STUDY; CRUSTACEA; ENTHALPY; EQUILIBRIUM CONSTANT; HEMOLYMPH; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION;

ANIMALS; ASTACOIDEA; BINDING SITES; CALORIMETRY; HEMOCYANIN; MODELS, CHEMICAL; THERMODYNAMICS; URIC ACID;

EID: 0035907116     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(01)00150-8     Document Type: Article

References (34)

1. Salvato B., Beltramini M. Hemocyanins: molecular architecture, structure and reactivity of the binuclear copper site. Life Chem. Rep. 8:1990;1-47.
2. Markl J., Decker H. Molecular structure of arthropod hemocyanins. Adv. Comp. Environ. Physiol. 13:1992;325-376.
3. van Holde K.E., Miller K.A. Hemocyanins. Adv. Protein Chem. 47:1995;1-81.
4. Ellerton H.D., Ellerton N.F., Robinson H.A. Hemocyanin - a current perspective. Prog. Biophys. Mol. Biol. 41:1983;143-248.
5. Robert C.H., Decker H., Richey B., Gill S.J., Wyman J. Nesting: hierarchies of allosteric interaction. Proc. Natl. Acad. Sci. USA. 84:1987;1891-1895.
6. Decker H., Sterner R. Nested allostery of arthropodan hemocyanin (Eurypelma californicum and Homarus vulgaris). J. Mol. Biol. 211:1990;281-293.
7. Magnus K.A., Hazes B., Ton-That H., Bonaventura C., Bonaventura J., Hol W.G.J. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins. 19:1994;302-309.
8. Hazes B., Magnus K.A., Bonaventura C., et al. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Protein Sci. 2:1993;597-619.
9. Gaykema W.P., Volbeda A., Hol W.G.J. Structure determination of Panulirus interruptus haemocyanin at 3.2 Å resolution. J. Mol. Biol. 197:1986;255-275.
10. Volbeda A., Hol W.G.J. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J. Mol. Biol. 209:1989;249-279.
11. Heel M.van, Dube P. Quaternary structure of multihexameric arthropod hemocyanins. Micron. 25:1994;387-418.
12. Stöcker W., Raeder U., Bijolt M.M., Wichertjes T., van Bruggen E.F.J., Markl J. The quaternary structure of four crustacean two-hexameric hemocyanins: immunocorrelation, stoichiometry, reassembly and topology of individual subunits. J. Comp. Physiol. B. 158:1988;271-289.
13. Truchot J.P., Lallier F.H. Modulation of the oxygen-carrying function of hemocyanin in crustaceans. News Physiol. Sci. 7:1992;49-52.
14. Truchot J.P. Lactate increases the oxygen affinity of crab hemocyanin. J. Exp. Zool. 214:1980;205-208.
15. Morris S., Bridges C.R., Grieshaber M.K. A new role for uric acid: modulator of haemocyanin oxygen affinity in crustaceans. J. Exp. Zool. 235:1985;135-139.
16. Lallier F., Truchot J.P. Hemolymph oxygen transport during environmental hypoxia in the shore crab, Carcinus maenas. Respir. Physiol. 77:1989;323-336.
17. Morris S., Bridges C.R., Grieshaber M.K. The potentiating effect of purine bases and some of their derivatives on the oxygen affinity of haemocyanin from the crayfish Austropotamobius pallipes. J. Comp. Physiol. B. 156:1986;431-440.
18. Morris S. Organic ions as modulators of respiratory pigment function during stress. Physiol. Zool. 63:1990;253-287.
19. Morris S., McMahon B.R. Potentation of hemocyanin oxygen affinity by catecholamines in the crab Cancer magister: a specific effect of dopamin. Physiol. Zool. 62:1989;654-667.
20. 2 affinity in a brachyuran hydrothermal crab. Mar. Biol. 113:1992;175-180.
21. Johnson B.A., Bonaventura C., Bonaventura J. Allostery in Callinectes sapidus hemocyanin: cooperative oxygen binding and interactions with L-lactate, calcium, and protons. Biochemistry. 27:1988;1995-2001.
22. Arisaka F., van Holde K.E. Allosteric properties and the association equilibria of hemocyanin from Callianassa californiensis. J. Mol. Biol. 134:1979;41-73.
23. Brouwer M., Serigstad B. Allosteric control in Limulus polyphemus hemocyanin: functional relevance of interactions between hexamers. Biochem. J. 28:1989;8819-8827.
24. Menze M., Hellmann N., Decker H., Grieshaber M. Binding of urate and caffeine to haemocyanin of the lobster Homarus vulgaris (E.) studied by isothermal titration calorimetry. Biochemistry. 39:2000;10806-10811.
25. Nies A., Zeis B., Bridges C.R., Grieshaber M.K. Allosteric modulation of haemocyanin oxygen-affinity by L-lactate and urate in the lobster Homarus vulgaris. II. Characterization of specific effector binding sites. J. Exp. Biol. 168:1992;111-124.
26. Scheibe P., Bernt E., Bergmeyer H.U. Methoden der enzymatischen Analyse. 1974;Verlag Chemie, Weinheim, Germany.
27. Wiseman T., Williston S., Brandts J.F., Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
28. Freire E., Mayorga O.L., Straume M. Isothermal titration calorimetry. Anal. Chem. 62:1990;949b-950a.
29. Ladbury J.E., Chowdry B.Z. Sensing the heat-the application of Isothermal Titration Calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol. 3:1996;791-801.
30. Fritzsche H., Petri I., Schutz H., Weller K., Sedmera P., Lang H. On the interaction of caffeine with nucleid acids. III. Biophys. Chem. 11:1980;109-119.
31. Dykens A.J. Purineolytic capacity and origin of hemolymph urate in Carcinus maenas during hypoxia. Comp. Biochem. Physiol. B. 98:1991;579-582.
32. Perutz M.F., Fermi G., Abrahan D.J., Poyart C., Bursaux E. Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding. J. Am. Chem. Soc. 108:1986;1064-1078.
33. Czytrich H.M., Bridges C.R., Grieshaber M. Purinstoffwechsel von Astacus leptodactylus. Verh. Deut. Zool. Ges. 80:1987;207.
34. Terada T.P., Kuwajima K. Thermodynamics of nucleotide binding to the chaperonin GroEL studies by isothermal titration calorimetry: evidence for noncooperative nucleotide binding. Biochim. Biophys. Acta. 1421:1999;269-281.