Altered heme environments in opossum and rabbit methemoglobins

Maliyakal E. John, Raymond N. DuBois, Michael R. Waterman

    Research output: Contribution to journalArticlepeer-review

    2 Scopus citations

    Abstract

    The effect of pH and inositol hexaphosphate (IHP) on the symmetry of the heme environments in opossum (Didelphius marsupialis) and New Zealand White rabbit hemoglobins has been studied using electron spin resonance (ESR). Each methemoglobin is found to contain two different heme environments as detected by the rhombicity observed in the ESR spectrum. In both cases the rhombic nature of the ESR spectrum is influenced by pH and IHP binding, although in the case of rabbit methemoglobin the high spin ESR signal disappears above pH 8.0. In both hemoglobins, amino acid alterations in the α-chains are known to affect the properties of the ferrous derivatives. It is concluded that these alterations also provide the basis for the ESR spectral properties observed with the methemoglobins.

    Original languageEnglish (US)
    Pages (from-to)964-967
    Number of pages4
    JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
    Volume36
    Issue number11-12
    DOIs
    StatePublished - Dec 1 1981

    Keywords

    • ESR
    • Heme Environment
    • Inositol Hexaphosphate
    • Methemoglobin
    • Spin State

    ASJC Scopus subject areas

    • Biochemistry, Genetics and Molecular Biology(all)

    Fingerprint Dive into the research topics of 'Altered heme environments in opossum and rabbit methemoglobins'. Together they form a unique fingerprint.

    Cite this