TY - JOUR
T1 - A proton magnetic relaxation study of ferric myoglobin and haemoglobin in water/ethanediol solutions
AU - Vuk-Pavlović, S.
AU - Bračika, V.
AU - Benko, B.
AU - Maričič, S.
N1 - Funding Information:
This work was supported by NIH PL-480 programme (grant 02-1304-1) and, in part, by the Science Association of the SR Croatia.
PY - 1977/4/25
Y1 - 1977/4/25
N2 - 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.
AB - 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.
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U2 - 10.1016/0005-2795(77)90287-2
DO - 10.1016/0005-2795(77)90287-2
M3 - Article
C2 - 15623
AN - SCOPUS:0017782762
SN - 1570-9639
VL - 491
SP - 447
EP - 456
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 2
ER -