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

doi:10.1007/BF00183533

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

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9 Scopus citations

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.

Original language	English
Pages (from-to)	253-256
Number of pages	4
Journal	European Biophysics Journal
Volume	19
Issue number	5
DOIs	https://doi.org/10.1007/BF00183533
State	Published - Mar 1991
Externally published	Yes

Keywords

Hemoglobin
Mössbauer-spectroscopy
Protein dynamics

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10.1007/BF00183533

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title = "Hemoglobin dynamics in rat erythrocytes investigated by M{\"o}ssbauer spectroscopy",

abstract = "Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. M{\"o}ssbauer 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.",

keywords = "Hemoglobin, M{\"o}ssbauer-spectroscopy, Protein dynamics",

author = "Frolov, {E. N.} and M. Fischer and E. Graffweg and Mirishly, {M. A.} and Goldanskii, {V. I.} and Parak, {F. G.}",

year = "1991",

month = mar,

doi = "10.1007/BF00183533",

language = "English",

volume = "19",

pages = "253--256",

journal = "European Biophysics Journal",

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T1 - Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy

AU - Frolov, E. N.

AU - Fischer, M.

AU - Graffweg, E.

AU - Mirishly, M. A.

AU - Goldanskii, V. I.

AU - Parak, F. G.

PY - 1991/3

Y1 - 1991/3

N2 - 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.

AB - 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.

KW - Hemoglobin

KW - Mössbauer-spectroscopy

KW - Protein dynamics

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U2 - 10.1007/BF00183533

DO - 10.1007/BF00183533

M3 - Article

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AN - SCOPUS:0026036476

SN - 0175-7571

VL - 19

SP - 253

EP - 256

JO - European Biophysics Journal

JF - European Biophysics Journal

IS - 5

ER -

Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy

Abstract

Keywords

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