Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.
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.
D000328:Adult; D002263:Carboxyhemoglobin / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000097:blood*; D007700:Kinetics; D008024:Ligands; D010108:Oxyhemoglobins / Q000378:metabolism; D011485:Protein Binding; D013057:Spectrum Analysis / Q000379:methods
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; D002263:Carboxyhemoglobin; D007501:Iron