Abstract
The effect of hydrogen ion, chloride, and 2,3-diphosphoglycerate upon the oxygen binding of hemoglobin may be satisfactorily described by an allosteric model employing three affinity states. The allosteric two-state model does not provide even an approximate description except under defined extreme conditions. In particular, the two-state model cannot provide a correct interpretation of recently reported electron spin resonance and nuclear magnetic resonance data.
Keywords: oxygen binding, affinity states, effector substances
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arnone A. X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin. Nature. 1972 May 19;237(5351):146–149. doi: 10.1038/237146a0. [DOI] [PubMed] [Google Scholar]
- Imai K. Analyses of oxygen equilibria of native and chemically modified human adult hemoglobins on the basis of Adair's stepwise oxygenation theory and the allosteric model of Monod, Wyman, and Changeux. Biochemistry. 1973 Feb 27;12(5):798–808. doi: 10.1021/bi00729a003. [DOI] [PubMed] [Google Scholar]
- Imai K., Tyuma I. Thermodynamical analysis of oxygen equilibrium of stripped hemoglobin. Biochem Biophys Res Commun. 1973 Mar 5;51(1):52–58. doi: 10.1016/0006-291x(73)90506-8. [DOI] [PubMed] [Google Scholar]
- Koshland D. E., Jr, Némethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 1966 Jan;5(1):365–385. doi: 10.1021/bi00865a047. [DOI] [PubMed] [Google Scholar]
- MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
- Ogata R. T., McConnell H. M. States of hemoglobin in solution. Biochemistry. 1972 Dec 5;11(25):4792–4799. doi: 10.1021/bi00775a024. [DOI] [PubMed] [Google Scholar]
- Ogata R. T., McConnell H. M. The binding of a spin-labeled triphosphate to hemoglobin. Cold Spring Harb Symp Quant Biol. 1972;36:325–336. doi: 10.1101/sqb.1972.036.01.043. [DOI] [PubMed] [Google Scholar]
- Ogawa S., Shulman R. G. High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactions. J Mol Biol. 1972 Sep 28;70(2):315–336. doi: 10.1016/0022-2836(72)90542-6. [DOI] [PubMed] [Google Scholar]
- Saroff H. A., Yap W. T. The action of hemoglobin. Cooperative effects in tetrameric proteins. Biopolymers. 1972;11(5):957–971. doi: 10.1002/bip.1972.360110504. [DOI] [PubMed] [Google Scholar]
- Shulman R. G., Ogawa S., Hopfield J. J. An allosteric model of hemoglobin. II. The assumption of independent binding. Arch Biochem Biophys. 1972 Jul;151(1):68–74. doi: 10.1016/0003-9861(72)90474-2. [DOI] [PubMed] [Google Scholar]
- Shulman R. G., Ogawa S., Hopfield J. J. An allosteric model of hemoglobin. Cold Spring Harb Symp Quant Biol. 1972;36:337–341. doi: 10.1101/sqb.1972.036.01.044. [DOI] [PubMed] [Google Scholar]
- Tyuma I., Imai K., Shimizu K. Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates. Biochemistry. 1973 Apr 10;12(8):1491–1498. doi: 10.1021/bi00732a004. [DOI] [PubMed] [Google Scholar]
- Tyuma I., Kamigawara Y., Imai K. PH dependence of the shape of the hemoglobin-oxygen equilibrium curve. Biochim Biophys Acta. 1973 Jun 15;310(2):317–320. doi: 10.1016/0005-2795(73)90111-6. [DOI] [PubMed] [Google Scholar]