Altered heme environments in opossum and rabbit methemoglobins

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

Research output: Contribution to journalArticle

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)

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