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Michael Waterman
Faculty Member
Last active: 2/12/2015

Altered heme environments in opossum and rabbit methemoglobins.

John ME, DuBois RN, Waterman MR
Z Naturforsch C Biosci. 1981 36 (11-12): 964-7

PMID: 6275619 · DOI:10.1515/znc-1981-11-1211

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 alpha-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.

MeSH Terms (13)

Animals Binding Sites Electron Spin Resonance Spectroscopy Heme Hemoglobin M Humans Hydrogen-Ion Concentration Methemoglobin Opossums Phytic Acid Protein Binding Protein Conformation Rabbits

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