ISSN:
1432-1017
Keywords:
Hemoglobin
;
Protein dynamics
;
Mössbauer-spectroscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. Mössbauer absorption spectroscopy on the hemoglobin of these erythrocytes has shown rather similar dynamics as found earlier in crystals of myoglobin, in frozen solutions of human hemoglobin and in a number of other proteins. The results strongly indicate that the motion of the heme and presumably some part of the F-helix is mainly influenced by the average viscosity of the sample determined by a network of hydrogen bridges and other weak interactions. Extrapolations of Mossbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00183533
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