Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy

✍ Scribed by E. N. Frolov; M. Fischer; E. Graffweg; M. A. Mirishly; V. I. Goldanskii; F. G. Parak

• Book ID: 104654343
• Publisher: Springer
• Year: 1991
• Tongue: English
• Weight: 320 KB
• Volume: 19
• Category: Article
• ISSN: 1432-1017
• DOI: 10.1007/bf00183533

✦ Synopsis

Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. M6ssbauer 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 heine 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 M6ssbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.