What the intermediate compounds in ligand binding to hemoglobin tell about the mechanism of cooperativity

Michele Perrella, Alfredo Colosimo, Louise Benazzi, Marilena Ripamonti, Luigi Rossi-Bernardi

Research output: Contribution to journalArticlepeer-review

Abstract

The populations of the intermediates in concentrated solutions of hemoglobin A0 equilibrated at various PCO values, pH 7.0, 0.1 M KCl, and 20 ° C, have been determined using cryogenic methods. Data on CO saturations and distributions of intermediates were analysed in terms of the free energies of dimer-tetramer assembly of the intermediates (G.K. Ackers and F.R. Smith, Annu. Rev. Biophys. Chem. 16 (1987) 583). The cooperative free energy value of the singly ligated species was approximately one-half the total cooperative energy. The cooperative free energy value of the doubly ligated species was not significantly different from that of carboxyhemoglobin. Because of experimental error, the observed difference in concentrations among the populations of the doubly ligated species cannot be taken as indicative of their functional heterogeneity. Additional studies on some NO intermediates have emphasized that (α1β1)(α2β2)X, a key intermediate in the formulation of the 'third-state' hypothesis in the deoxy/cyanomethemoglobin system, has a free energy value for dimer-tetramer assembly which is critically dependent on the nature of the ligand X as suggested by Ackers and Smith (reference as cited above).

Original languageEnglish
Pages (from-to)211-223
Number of pages13
JournalBiophysical Chemistry
Volume37
Issue number1-3
DOIs
Publication statusPublished - Aug 31 1990

Keywords

  • Allosterism
  • Cryogenics
  • Hemoglobin intermediate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Physical and Theoretical Chemistry

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