Modulation of oxygen affinity in hemoglobin by solvent components. Interaction of bovine hemoglobin with 2,3-diphosphoglycerate and monatomic anions

Clara Fronticelli, Enrico Bucci, Anna Razynska

Research output: Contribution to journalArticlepeer-review

Abstract

In the absence of Cl- in Hepes buffer at pH 7.4, the oxygen affinity of bovine and human hemoglobin is equally sensitive to 2,3-diphosphoglyceric acid. The low oxygen affinity measured for bovine hemoglobin at physiological salt concentration can be explained by the high affinity of Cl- anions for oxygen-linked sites that are absent in human hemoglobin. Bovine hemoglobin can discriminate between the different halogens in the sense that different halide concentrations are necessary to produce the same P50. Competition experiments indicate that the halogens interact with the same oxygen-linked sites. In agreement with the different affinities for halides, the Bohr effect of bovine hemoglobin is larger in the presence of Cl- than in that of Br- and there is good agreement between the number of protons and anions exchanged with the solvent upon oxygenation of bovine hemoglobin.

Original languageEnglish (US)
Pages (from-to)343-348
Number of pages6
JournalJournal of molecular biology
Volume202
Issue number2
DOIs
StatePublished - Jul 20 1988
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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