Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy

Biophys J. 1985 Dec;48(6):997-1001. doi: 10.1016/S0006-3495(85)83862-5.

Abstract

K-absorption edge of coordinated ions exhibits a fine structure (through the use of XANES, or x-ray absorption near edge structures) that reflects the electronic repartition and the chemical reactivity of these ions. Comparative analysis of iron K-absorption-edge shape for hemoglobin derivatives with different ligand affinity suggests strongly that in hemoglobin, iron-forms with high and low affinity are highly improbable.

MeSH terms

  • Adult
  • Carboxyhemoglobin / metabolism
  • Hemoglobins / metabolism*
  • Humans
  • Hydrogen-Ion Concentration
  • Iron / blood*
  • Kinetics
  • Ligands
  • Oxyhemoglobins / metabolism
  • Protein Binding
  • Spectrum Analysis / methods

Substances

  • Hemoglobins
  • Ligands
  • Oxyhemoglobins
  • Carboxyhemoglobin
  • Iron