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Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.
Biophys J ; 48(6): 997-1001, 1985 Dec.
Article em En | MEDLINE | ID: mdl-4092074
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hemoglobinas / Ferro Limite: Adult / Humans Idioma: En Revista: Biophys J Ano de publicação: 1985 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hemoglobinas / Ferro Limite: Adult / Humans Idioma: En Revista: Biophys J Ano de publicação: 1985 Tipo de documento: Article