Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy
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 prote...
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| Veröffentlicht in: | European biophysics journal 1991-01, Vol.19 (5), p.253-256 |
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| container_title | European biophysics journal |
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| creator | FROLOV, E. N FISCHER, M GRAFFWEG, E MIRISHLY, M. A GOLDANSKII, V. I PARAK, F. G |
| 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. |
| doi_str_mv | 10.1007/BF00183533 |
| format | Article |
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Extrapolations of Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/BF00183533</identifier><identifier>PMID: 2060496</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Animals ; Biological and medical sciences ; Conformational dynamics in molecular biology ; Erythrocytes - metabolism ; Fundamental and applied biological sciences. 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N</creatorcontrib><creatorcontrib>FISCHER, M</creatorcontrib><creatorcontrib>GRAFFWEG, E</creatorcontrib><creatorcontrib>MIRISHLY, M. A</creatorcontrib><creatorcontrib>GOLDANSKII, V. I</creatorcontrib><creatorcontrib>PARAK, F. G</creatorcontrib><title>Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><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.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Conformational dynamics in molecular biology</subject><subject>Erythrocytes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heme - metabolism</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - metabolism</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Molecular biophysics</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>Spectroscopy, Mossbauer</subject><issn>0175-7571</issn><issn>1432-1017</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LxEAMhgdR1nX14l3oRW_VTKfzddTFVWFlL3ou02m6VvrlzFToH_MP-MesWMwhCXkfXpIQck7hmgLIm7sNAFWMM3ZAljRlSUyBykOynDKPJZf0mJx4_w6QckrVgiwSEJBqsSS7R2y6fd3lVRsVY2uayvpo6p0JEboxvLnOjgF_Z5_oQ7U3AYsoH6Pn7y_vczOgi3yPNrjO264fT8lRaWqPZ3NdkdfN_cv6Md7uHp7Wt9u4T5gIMbdaA4DIBeO5miJXpVUsNSXFRNsk0aDBKClLDkJwi8wmtEgV1VopRMZW5OrPt3fdxzBtljWVt1jXpsVu8JkCMd0H6QRezOCQN1hkvasa48Zs_sCkX8668dbUpTOtrfw_RrXUEiRjPy2waeA</recordid><startdate>19910101</startdate><enddate>19910101</enddate><creator>FROLOV, E. 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N</creatorcontrib><creatorcontrib>FISCHER, M</creatorcontrib><creatorcontrib>GRAFFWEG, E</creatorcontrib><creatorcontrib>MIRISHLY, M. A</creatorcontrib><creatorcontrib>GOLDANSKII, V. I</creatorcontrib><creatorcontrib>PARAK, F. G</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>European biophysics journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>FROLOV, E. N</au><au>FISCHER, M</au><au>GRAFFWEG, E</au><au>MIRISHLY, M. A</au><au>GOLDANSKII, V. I</au><au>PARAK, F. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy</atitle><jtitle>European biophysics journal</jtitle><addtitle>Eur Biophys J</addtitle><date>1991-01-01</date><risdate>1991</risdate><volume>19</volume><issue>5</issue><spage>253</spage><epage>256</epage><pages>253-256</pages><issn>0175-7571</issn><eissn>1432-1017</eissn><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 Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>2060496</pmid><doi>10.1007/BF00183533</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 0175-7571 |
| ispartof | European biophysics journal, 1991-01, Vol.19 (5), p.253-256 |
| issn | 0175-7571 1432-1017 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Animals Biological and medical sciences Conformational dynamics in molecular biology Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology Heme - metabolism Hemoglobins - chemistry Hemoglobins - metabolism Iron - metabolism Kinetics Molecular biophysics Protein Conformation Rats Spectroscopy, Mossbauer |
| title | Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy |
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