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. 1965 Aug;54(2):535–542. doi: 10.1073/pnas.54.2.535

Subunit exchange and ligand binding: a new hypothesis for the mechanism of oxygenation of hemoglobin.

R E Benesch, R Benesch, G Macduff
PMCID: PMC219700  PMID: 5217440

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ACKERS G. K., THOMPSON T. E. DETERMINATION OF STOICHIOMETRY AND EQUILIBRIUM CONSTANTS FOR REVERSIBLY ASSOCIATING SYSTEMS BY MOLECULAR SIEVE CHROMATOGRAPHY. Proc Natl Acad Sci U S A. 1965 Feb;53:342–349. doi: 10.1073/pnas.53.2.342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ANTONINI E., WYMAN J., BRUNORI M., BUCCI E., FRONTICELLI C., ROSSI-FANELLI A. STUDIES ON THE RELATIONS BETWEEN MOLECULAR AND FUNCTIONAL PROPERTIES OF HEMOGLOBIN. IV. THE BOHR EFFECT IN HUMAN HEMOGLOBIN MEASURED BY PROTON BINDING. J Biol Chem. 1963 Sep;238:2950–2957. [PubMed] [Google Scholar]
  3. ANTONINI E., WYMAN J., BRUNORI M., TAYLOR J. F., ROSSI-FANELLI A., CAPUTO A. STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN. J Biol Chem. 1964 Mar;239:907–912. [PubMed] [Google Scholar]
  4. ANTONINI E., WYMAN J., BUCCI E., FRONTICELLI C., ROSSI-FANELLI A. The dissociation and recombination of subunits of human, horse, and canine hemoglobin. J Mol Biol. 1962 May;4:368–375. doi: 10.1016/s0022-2836(62)80017-5. [DOI] [PubMed] [Google Scholar]
  5. ATKINSON D. E., HATHAWAY J. A., SMITH E. C. KINETICS OF REGULATORY ENZYMES. KINETIC ORDER OF THE YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE ISOCITRATE DEHYDROGENASE REACTION AND A MODEL FOR THE REACTION. J Biol Chem. 1965 Jun;240:2682–2690. [PubMed] [Google Scholar]
  6. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. BENESCH R. E., BENESCH R., MACDUFF G. THE DISSOCIATION OF HEMOGLOBINS A AND H IN CONCENTRATED SODIUM CHLORIDE. Biochemistry. 1964 Aug;3:1132–1135. doi: 10.1021/bi00896a021. [DOI] [PubMed] [Google Scholar]
  8. BENESCH R. E., BENESCH R. The influence of oxygenation on the reactivity of the--SH groups of hemoglobin. Biochemistry. 1962 Sep;1:735–738. doi: 10.1021/bi00911a002. [DOI] [PubMed] [Google Scholar]
  9. BENESCH R. E., BENESCH R., WILLIAMSON M. E. The influence of reversible oxygen binding on the interaction between hemoglobin submits. Proc Natl Acad Sci U S A. 1962 Dec 15;48:2071–2075. doi: 10.1073/pnas.48.12.2071. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. BENESCH R., MACDUFF G., BENESCH R. E. DETERMINATION OF OXYGEN EQUILIBRIA WITH A VERSATILE NEW TONOMETER. Anal Biochem. 1965 Apr;11:81–87. doi: 10.1016/0003-2697(65)90045-x. [DOI] [PubMed] [Google Scholar]
  11. CHANGEUX J. P. ALLOSTERIC INTERACTIONS INTERPRETED IN TERMS OF QUATERNARY STRUCTURE. Brookhaven Symp Biol. 1964 Dec;17:232–249. [PubMed] [Google Scholar]
  12. Douglas C. G., Haldane J. S., Haldane J. B. The laws of combination of haemoglobin with carbon monoxide and oxygen. J Physiol. 1912 Jun 12;44(4):275–304. doi: 10.1113/jphysiol.1912.sp001517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GIBSON Q. H. The photochemical formation of a quickly reacting form of haemoglobin. Biochem J. 1959 Feb;71(2):293–303. doi: 10.1042/bj0710293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. GUIDOTTI G., CRAIG L. C. Dialysis studies. VIII. The behavior of solutes which associate. Proc Natl Acad Sci U S A. 1963 Jul;50:46–54. doi: 10.1073/pnas.50.1.46. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. HUISMAN T. H., DOZY A. M. Studies on the heterogeneity of hemoglobin. V. Binding of hemoglobin with oxidized glutathione. J Lab Clin Med. 1962 Aug;60:302–319. [PubMed] [Google Scholar]
  16. 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]
  17. MUIRHEAD H., PERUTZ M. F. STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION. Nature. 1963 Aug 17;199:633–638. doi: 10.1038/199633a0. [DOI] [PubMed] [Google Scholar]
  18. PERUTZ M. F., BOLTON W., DIAMOND R., MUIRHEAD H., WATSON H. C. STRUCTURE OF HAEMOGLOBIN. AN X-RAY EXAMINATION OF REDUCED HORSE HAEMOGLOBIN. Nature. 1964 Aug 15;203:687–690. doi: 10.1038/203687a0. [DOI] [PubMed] [Google Scholar]
  19. RIGGS A. The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium. J Biol Chem. 1961 Jul;236:1948–1954. [PubMed] [Google Scholar]
  20. SCHEJTER A., ADLER A. D., GLAUSER S. C. STOICHIOMETRY OF HEMOGLOBIN REACTIONS. Science. 1963 Aug 30;141(3583):784–788. doi: 10.1126/science.141.3583.784. [DOI] [PubMed] [Google Scholar]
  21. WEISS J. J. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN. Nature. 1964 Apr 4;202:83–84. doi: 10.1038/202083b0. [DOI] [PubMed] [Google Scholar]

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