Asymmetric [deoxy dimer/azido-met dimer] hemoglobin hybrids dissociate within seconds

Journal of Molecular Biology

Volumn 291, Issue 1, 1999, Pages 227-236

  Kiger, L ^a   Marden, M C ^a  

^a INSERM   (France)

Author keywords

Allosteric regulation; Hemoglobin; Ligand binding; Protein conformation; Stopped flow kinetics

Indexed keywords

AZIDE; CARBON MONOXIDE; DEOXYHEMOGLOBIN; DIMER; DITHIONITE; HEMOGLOBIN; LIGAND; METHEMOGLOBIN; OXYGEN; OXYHEMOGLOBIN; TETRAMER;

ALLOSTERISM; ARTICLE; HYBRID; LIGAND BINDING; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN STABILITY;

EID: 0344500750     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2970     Document Type: Article

References (26)

1. Ackers G. K., Doyle M. L., Myers D., Daugherty M. A. Molecular code for cooperativity in hemoglobin. Science. 255:1992;54-63.
2. +CN)( αβ): methodological and mechanistic issues. Biochemistry. 36:1997;10822-10829.
3. Cassoly R. Preparation of hemoglobin hybrids carrying different ligands: valency hybrids and related compounds. Methods Enzymol. 76:1981;106-113.
4. Chu A. H., Ackers G. K. Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect. J. Biol. Chem. 256:1981;1199-1205.
5. Daugherty M. A., Shea M. A., Ackers G. K. Bohr effects of the partially-ligated (CN-met) intermediates of hemoglobin as probed by quaternary assembly. Biochemistry. 33:1994;10345-10357.
6. 2binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. Biophys. Chem. 64:1997;271-287.
7. Eaton W. A., Henry E. R., Hofrichter J., Mozzarelli A. Is cooperative oxygen binding by hemoglobin really understood? Nature Struct. Biol. 6:1999;351-358.
8. Gibson Q. H., Parkhurst L. J., Geraci G. The reaction of methemoglobin with some ligands. J. Biol. Chem. 244:1969;4668-4676.
9. Huang Y., Yonetani T., Tsuneshige A., Hoffman B. M., Ackers G. K. Heterometallic hybrids of homometallic human hemoglobins. Proc. Natl Acad. Sci. USA. 93:1996a;4425-4430.
10. Huang Y., Doyle M. L., Ackers G. K. The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids. Biophys. J. 71:1996b;2094-2105.
11. Kiger L., Poyart C., Marden M. C. CO binding and valency exhange in asymmetric deoxy/azide hemoglobin hybrids. Biochemistry. 37:1998;14643-14650.
12. LiCata V. J., Dalessio P. M., Ackers G. K. Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. Proteins: Struct. Funct. Genet. 17:1993;279-296.
13. Marden M. C., Griffon N., Poyart C. Asymmetric hybrids of hemoglobin. J. Mol. Biol. 263:1996;90-97.
14. Marden M. C., Kiger L., Poyart C., Edelstein S. J. Identifying the conformational state of bi-liganded hemoglobin. Cell. Mol. Life Sci. 54:1998;1365-1384.
15. Monod J., Wyman J., Changeux J. P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:1965;81-118.
16. Nagel R. L., Gibson Q. H. The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J. Biol. Chem. 246:1971;69-73.
17. Parkhurst K. M., Parkhurst L. J. Rapid preparation of native alpha and beta chains of human hemoglobin. Int. J. Biochem. 24:1992;993-998.
18. Perrella M., Benazzi L., Shea M. A., Ackers G. K. Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states. Biophys. Chem. 35:1990;97-103.
19. Perrella M., Davids N., Rossi-Bernardi L. The association reaction between hemoglobin and carbon monoxide as studied by the isolation of the intermediates. Implications on the mechanism of cooperativity. J. Biol. Chem. 267:1992;8744-8751.
20. Philo J. S., Dreyer U., Lary J. W. Quaternary structure dynamics and carbon monoxide binding kinetics of hemoglobin valency hybrids. Biophys. J. 70:1996;1949-1965.
21. Sawicki C. A., Gibson Q. H. Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. J. Biol. Chem. 251:1976;1533-1542.
22. 2CO. J. Biol. Chem. 263:1988;2292-2298.
23. 1. J. Biol. Chem. 264:1989;10582-10588.
24. +CN-)(αβ): no preferentially populating asymmetric hybrid at equilibrium. Biochemistry. 36:1997;4375-4381.
25. +CN-)(αβ): the issue of valency exchange. Biochemistry. 37:1998;6221-6228.
26. Winterhalter K. H., Colosimo A. Chromatographic isolation and characterization of isolated chains from hemoglobin after regeneration of sulfhydryl groups. Biochemistry. 10:1971;621-624.