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Magnetic mechanism for the biological functioning of hemoglobin
The role of magnetism in the biological functioning of hemoglobin has been debated since its discovery by Pauling and Coryell in 1936. The hemoglobin molecule contains four heme groups each having a porphyrin layer with a Fe ion at the center. Here, we present combined density-functional theory and...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7244595/ https://www.ncbi.nlm.nih.gov/pubmed/32444622 http://dx.doi.org/10.1038/s41598-020-64364-y |
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author | Mayda, Selma Kandemir, Zafer Bulut, Nejat Maekawa, Sadamichi |
author_facet | Mayda, Selma Kandemir, Zafer Bulut, Nejat Maekawa, Sadamichi |
author_sort | Mayda, Selma |
collection | PubMed |
description | The role of magnetism in the biological functioning of hemoglobin has been debated since its discovery by Pauling and Coryell in 1936. The hemoglobin molecule contains four heme groups each having a porphyrin layer with a Fe ion at the center. Here, we present combined density-functional theory and quantum Monte Carlo calculations for an effective model of Fe in a heme cluster. In comparison with these calculations, we analyze the experimental data on human adult hemoglobin (HbA) from the magnetic susceptibility, Mössbauer and magnetic circular dichroism (MCD) measurements. In both the deoxygenated (deoxy) and the oxygenated (oxy) cases, we show that local magnetic moments develop in the porphyrin layer with antiferromagnetic coupling to the Fe moment. Our calculations reproduce the magnetic susceptibility measurements on deoxy and oxy-HbA. For deoxy-HbA, we show that the anomalous MCD signal in the UV region is an experimental evidence for the presence of antiferromagnetic Fe-porphyrin correlations. The functional properties of hemoglobin such as the binding of O(2), the Bohr effect and the cooperativity are explained based on the magnetic correlations. This analysis suggests that magnetism could be involved in the functioning of hemoglobin. |
format | Online Article Text |
id | pubmed-7244595 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72445952020-05-30 Magnetic mechanism for the biological functioning of hemoglobin Mayda, Selma Kandemir, Zafer Bulut, Nejat Maekawa, Sadamichi Sci Rep Article The role of magnetism in the biological functioning of hemoglobin has been debated since its discovery by Pauling and Coryell in 1936. The hemoglobin molecule contains four heme groups each having a porphyrin layer with a Fe ion at the center. Here, we present combined density-functional theory and quantum Monte Carlo calculations for an effective model of Fe in a heme cluster. In comparison with these calculations, we analyze the experimental data on human adult hemoglobin (HbA) from the magnetic susceptibility, Mössbauer and magnetic circular dichroism (MCD) measurements. In both the deoxygenated (deoxy) and the oxygenated (oxy) cases, we show that local magnetic moments develop in the porphyrin layer with antiferromagnetic coupling to the Fe moment. Our calculations reproduce the magnetic susceptibility measurements on deoxy and oxy-HbA. For deoxy-HbA, we show that the anomalous MCD signal in the UV region is an experimental evidence for the presence of antiferromagnetic Fe-porphyrin correlations. The functional properties of hemoglobin such as the binding of O(2), the Bohr effect and the cooperativity are explained based on the magnetic correlations. This analysis suggests that magnetism could be involved in the functioning of hemoglobin. Nature Publishing Group UK 2020-05-22 /pmc/articles/PMC7244595/ /pubmed/32444622 http://dx.doi.org/10.1038/s41598-020-64364-y Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Mayda, Selma Kandemir, Zafer Bulut, Nejat Maekawa, Sadamichi Magnetic mechanism for the biological functioning of hemoglobin |
title | Magnetic mechanism for the biological functioning of hemoglobin |
title_full | Magnetic mechanism for the biological functioning of hemoglobin |
title_fullStr | Magnetic mechanism for the biological functioning of hemoglobin |
title_full_unstemmed | Magnetic mechanism for the biological functioning of hemoglobin |
title_short | Magnetic mechanism for the biological functioning of hemoglobin |
title_sort | magnetic mechanism for the biological functioning of hemoglobin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7244595/ https://www.ncbi.nlm.nih.gov/pubmed/32444622 http://dx.doi.org/10.1038/s41598-020-64364-y |
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