6533b83afe1ef96bd12a713e

RESEARCH PRODUCT

Hemoglobin dynamics in rat erythrocytes investigated by M�ssbauer spectroscopy

V. I. GoldanskiiM. A. MirishlyM. FischerE. GraffwegFritz G. ParakE. N. Frolov

subject

ErythrocytesHemeproteinAbsorption spectroscopyProtein ConformationIronProtein dynamicsBiophysicsAnalytical chemistryHemeGeneral MedicineRatsHemoglobinsKineticsSpectroscopy MossbauerRed blood cellchemistry.chemical_compoundmedicine.anatomical_structureMyoglobinchemistrymedicineBiophysicsAnimalsHemoglobinProtein crystallizationHeme

description

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 Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.

https://doi.org/10.1007/bf00183533