Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy - Sorbonne Université
Article Dans Une Revue Biophysical Journal Année : 1985

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

Résumé

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.

Domaines

Chimie

Dates et versions

hal-04664645 , version 1 (30-07-2024)

Identifiants

Citer

S. Pin, P. Valat, Robert Cortès, A. Michalowicz, B. Alpert. Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy. Biophysical Journal, 1985, 48 (6), pp.997-1001. ⟨10.1016/S0006-3495(85)83862-5⟩. ⟨hal-04664645⟩
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