Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy

E. N. Frolov, M. Fischer, E. Graffweg, M. A. Mirishly, V. I. Goldanskii, F. G. Parak

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


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.

Original languageEnglish
Pages (from-to)253-256
Number of pages4
JournalEuropean Biophysics Journal
Issue number5
StatePublished - Mar 1991
Externally publishedYes


  • Hemoglobin
  • Mössbauer-spectroscopy
  • Protein dynamics


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