Changes in the Structural Ordering of Hemoglobin under Extreme Conditions of the Arctic Region

• Main Authors: V.G, Kunitsyn, L.E, Panin, L.P, Osipova, L.E, Tabikhanova, T.V, Churkina, A.A, Rozumenko
• Format: Article in Journal/Newspaper
• Language: English
• Published: Asian Economic and Social Society 2015
• Subjects: The arctic region; Hemoglobin structure; UV and IR fourier spectroscopy; Arctic; Yamal Peninsula
• Online Access: https://archive.aessweb.com/index.php/5003/article/view/3709

The structure of hemoglobin (Hb) was examined by UV and IR Fourier spectroscopy. The electronic characteristics of the -conjugated (aromatic) prosthetic group of heme and the content of the secondary structure elements of globin in Hb were studied. Heme and globin are connected to each other by Van der Waals forces. A 8-10 nm short-wave shift of the heme absorption band at 417±0.5 nm was revealed for the residents of the Arctic Region in different latitudes (the Yamal Peninsula, 64 and 70° North) as compared to the residents of middle latitudes (Novosibirsk, 55° North). This indicates that the ordering of heme structure increases with the latitude of human residence. The IR Fourier spectroscopy study of the content of the secondary structure elements showed that the ordering of hemoglobin in the Arctic residents increases with latitude. The study has demonstrated that affinity of Hb for oxygen in the residents of the Arctic Region is higher than in the residents of middle latitudes. Changes in the structure of Hb and its affinity for oxygen in the Arctic residents can be attributed to heliophysical factors.