A proton magnetic relaxation study of ferric myoglobin and haemoglobin in water/ethanediol solutions

S. Vuk-Pavlović, V. Bračika, B. Benko, S. Maričič

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Structural alterations of the haem vicinity of the high-spin derivatives of bovine ferric myoglobin (metmyoglobin) and human haemoglobin and the changes of the interaction with inositol hexaphosphate induced by ethanediol were monitored by solvent-proton magnetic relaxation. On addition of ethanediol up to 60% the fluoromet derivatives exhibit a gradual increase in the accessibility of the haem for the molecules from the solvent. In aquomethaemoglobin solutions with more than 25% ethanediol there is no unique explanation of proton magnetic relaxation. Ethanediol enhances the binding of inositol hexaphosphate to methaemoglobin, but the structural consequences of this binding on the haem-pockets seem to be diminished. The mechanisms of the observed structural and functional alterations of myoglobin as well as haemoglobin tetramer are discussed here.

Original languageEnglish (US)
Pages (from-to)447-456
Number of pages10
JournalBBA - Protein Structure
Volume491
Issue number2
DOIs
StatePublished - Apr 25 1977

ASJC Scopus subject areas

  • Medicine(all)

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