Effects of heterotropic allosteric effectors on the equilibrium and kinetics of the reaction of a single ligand molecule with an α or β subunit of deoxygenated HbA

Biochemistry

Volumn 43, Issue 24, 2004, Pages 7851-7856

  Karasik, Ellen ^a   Kwiatkowski, Laura D ^a   Hui, Hilda L ^a   Colby, Judith F ^a   Noble, Robert W ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; DISSOCIATION; HEMOGLOBIN; MOLECULAR DYNAMICS; REACTION KINETICS; THERMODYNAMICS;

ALLOSTERIC EFFECTORS; EQUILIBRIUM CONSTANTS;

BIOCHEMISTRY;

DEOXYHEMOGLOBIN; DEOXYHEMOGLOBIN A ALPHA; DEOXYHEMOGLOBIN A BETA; HEME; HEMOGLOBIN A; LIGAND; OXYGEN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; DISSOCIATION CONSTANT; EQUILIBRIUM CONSTANT; KINETICS; LIGAND BINDING; OXYGEN AFFINITY; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; THERMODYNAMICS;

ALLOSTERIC REGULATION; HEMOGLOBIN A; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; OXYGEN; THERMODYNAMICS;

EID: 2942717038     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0302649     Document Type: Article

References (18)

1. Monod, J., Wyman, J., and Changeux, J. P. (1965) On the nature of allosteric transitions: a plausible model, J. Mol. Biol. 12, 88-118.
2. Szabo, A., and Karplus, M. (1972) A mathematical model for structure-function relations in hemoglobin, J. Mol. Biol. 72, 163-197.
3. Minton, A. P., and Imai, K. (1974) The three-state model: a minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin, Proc. Natl. Acad. Sci. U.S.A. 71, 1418-1421.
4. Ackers, G. K. (1998) Deciphering the molecular code of hemoglobin allostery, Adv. Protein Chem. 51, 185-253.
5. Hui, H. L., Kwiatkowski, L. D., Karasik, E., Colby, J. E., and Noble, R. W. (2004) Ligand binding to symmetrical Fe-Zn hybrids of variants of human HbA with modifications in the α1β2 interface, Biochemistry 43, 7843-7850.
6. Imai, K., and Yonetani, T. (1975) pH dependence of the Adair constants of human hemoglobin, J. Biol. Chem. 250, 2227-2231.
7. Mozzarelli, A., Rivetti, C., Rossi, G. L., Eaton, W. A., and Henry, E. R. (1997) Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals, Protein Sci. 6, 484-489.
8. Rivetti, C., Mozzarelli, A., Rossi, G. R., Henry, E. R., and Eaton, W. A. (1993) Oxygen binding by single crystals of hemoglobin, Biochemistry 32, 2888-2906.
9. Noble, R. W., Hui, H. L., Kwiatkowski, L. D., Paily, P., DeYoung, A., Wierzba, A., and Colby, J. E. (2001) Mutational effects at the subunit interfaces of human hemoglobin: evidence for a unique sensitivity of the T quaternary state to changes in the hinge region of the α1β2 interface, Biochemistry 40, 12357-12368.
10. Doyle, M. L., Lew, G., De Young, A., Kwiatkowski, L., Wierzba, A., Noble, R. W., and Ackers, G. K. (1992) Functional properties of human hemoglobin synthesized from recombinant mutant beta-globins, Biochemistry 31, 8629-8639.
11. Atha, D. H., and Riggs, A. (1976) Tetramer-dimer dissociation in hemoglobin and the Bohr effect, J. Biol. Chem. 251, 5537-5543.
12. Ackers, G. K., Holt, J. M., Huang, Y., Grinkova, Y., Klinger, A. L., and Denisov, I. (2000) Confirmation of a unique intra-dimer cooperativity in the human hemoglobin α1β1 half-oxygenated intermediate supports the symmetry rule model of allosteric regulation, Proteins: Struct., Funct., Genet. Suppl. 4, 23-43.
13. Miyazaki, G., Morimoto, H., Yun, K.-M., Park, S.-Y., Nakagawa, A., Minagawa, H., and Shibayama, N. (1999) Magnesium(II) and Zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme, J. Mol. Biol. 292, 1121-1136.
14. Imai, K. (1982) Allosteric Effects in Hemoglobin, Cambridge University Press, Cambridge.
15. Noble, R. W., Kwiatkowski, L. D., Hui, H. L., Bruno, S., Bettati, S., and Mozzarelli, A. (2002) Correlation of protein functional properties in the crystal and in solution: the case study of T state hemoglobin, Protein Sci. 11, 1845-1849.
16. Yonetani, T., Park, S., Tsuneshige, A., Imai, K., and Kanaori, K. (2002) Global allostery model of hemoglobin: modulation of O(2) affinity, cooperativity and Bohr effect by heterotropic allosteric effectors, J. Biol. Chem. 277, 34508-34520.
17. Samuni, U., Juszczak, L., Dantsker, D., Khan, I., Friedman, A. J., Perez-Gonzalez-de-Apodeaca, J., Bruno, S., Hui, H. L., Colby, J. E., Karasik, E., Kwiatkowski, L. D., Mozzarelli, A., Noble, R. W., and Friedman, J. M. (2003) Functional and spectroscopic characterization of half-liganded iron-zinc hybrid hemoglobin: evidence for conformational plasticity within the T state, Biochemistry 42, 8272-8288.
18. Kilmartin, J. V., Imai, K., Jones, R. T., Faruqui, R., Fogg, J., and Baldwin, J. M. (1978) Role of Bohr group salt bridges in cooperativity in hemoglobin, Biochim. Biophys. Acta 534, 15-25.