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 Citations (Scopus)

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
Externally publishedYes

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Ethylene Glycols
Metmyoglobin
Magnetic relaxation
Protons
Hemoglobins
Heme
Phytic Acid
Water
Derivatives
Methemoglobin
Molecules

ASJC Scopus subject areas

  • Medicine(all)

Cite this

A proton magnetic relaxation study of ferric myoglobin and haemoglobin in water/ethanediol solutions. / Vuk-Pavlović, S.; Bračika, V.; Benko, B.; Maričič, S.

In: BBA - Protein Structure, Vol. 491, No. 2, 25.04.1977, p. 447-456.

Research output: Contribution to journalArticle

Vuk-Pavlović, S. ; Bračika, V. ; Benko, B. ; Maričič, S. / A proton magnetic relaxation study of ferric myoglobin and haemoglobin in water/ethanediol solutions. In: BBA - Protein Structure. 1977 ; Vol. 491, No. 2. pp. 447-456.
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