Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/8813
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dc.contributor.authorMayda, Selma-
dc.contributor.authorKandemir, Zafer-
dc.contributor.authorBulut, Nejat-
dc.contributor.authorMaekawa, Sadamichi-
dc.date.accessioned2020-07-18T08:31:27Z-
dc.date.available2020-07-18T08:31:27Z-
dc.date.issued2020-
dc.identifier.issn2045-2322-
dc.identifier.urihttps://doi.org/10.1038/s41598-020-64364-y-
dc.identifier.urihttps://hdl.handle.net/11147/8813-
dc.descriptionWOS: 000540510300072en_US
dc.descriptionPubMed: 32444622en_US
dc.description.abstractThe 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, Mossbauer 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.en_US
dc.language.isoenen_US
dc.publisherNature Publishing Groupen_US
dc.relation.ispartofScientific Reportsen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleMagnetic mechanism for the biological functioning of hemoglobinen_US
dc.typeArticleen_US
dc.departmentIzmir Institute of Technology. Physicsen_US
dc.departmentIzmir Institute of Technology. Materials Science and Engineeringen_US
dc.identifier.volume10en_US
dc.identifier.issue1en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.cont.department-temp[Mayda, Selma; Kandemir, Zafer; Bulut, Nejat] Izmir Inst Technol, Dept Phys, TR-35430 Urla, Turkey; [Mayda, Selma] Izmir Inst Technol, Dept Mat Sci & Engn, TR-35430 Urla, Turkey; [Maekawa, Sadamichi] RIKEN Ctr Emergent Matter Sci, Wako, Saitama 3510198, Japan; [Maekawa, Sadamichi] Univ Chinese Acad Sci, Kavli Inst Theoret Sci, Beijing 100049, Peoples R Chinaen_US
dc.identifier.doi10.1038/s41598-020-64364-y-
dc.relation.doi10.1038/s41598-020-64364-yen_US
dc.coverage.doi10.1038/s41598-020-64364-yen_US
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextnone-
crisitem.author.deptDepartment of Pyhsics-
Appears in Collections:PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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