Electronic state of iron in hemoglobin, myoglobin, and derivatives, as inferred from x-ray fluorescence spectra

A.S. Koster

    Research output: Contribution to journalArticleAcademicpeer-review

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    Abstract

    The Fe Kß fluorescence emission spectrum was used to study the coordination of iron in some heme proteins. The spectrum was found to be dependent only on the direct environment of the iron. The iron atom in oxyhemoglobin can be regarded as trivalent, with a considerable negative charge on the outer oxygen atom of the O2 ligand. Carbonmonoxide hemoglobin contains divalent, zero spin iron. Methemoglobin is a low spin compound.
    Original languageEnglish
    Pages (from-to)3161-3164
    Number of pages4
    JournalJournal of Chemical Physics
    Volume56
    Issue number6
    DOIs
    Publication statusPublished - 1972

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