Abstract —Using Raman spectroscopy (RS) approach in a spectral range of 1000–3000 cm –1 were used to study the conformational and structural changes that arise in the heme group and globin moiety of hemoglobin in human red blood cells at various temperatures and oxygen contents. In hypoxia, the hemoglobin conformation was shown to change as a result of the increasing contribution of hematoporphyrin pyrrole rings and vibrational motions of vinyl groups. Modifications were additionally detected in the contributions of symmetric and asymmetric vibrations of the CH 2 and CH 3 radicals of histidine (2850, 2860, and 2900 cm –1 ) and lysine (2880 and 2860 cm –1 ) residues. The mechanisms of oxygen binding are discussed for hemoglobin located in the submembrane region and cytoplasm of the cell.

中文翻译：

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温度变化和常压缺氧引起血红素和珠蛋白的构象变化

摘要——利用拉曼光谱 (RS) 方法在 1000-3000 cm-1 的光谱范围内研究了在不同温度和氧气下人红细胞中血红素基团和血红蛋白珠蛋白部分的构象和结构变化。内容。在缺氧条件下，由于血卟啉吡咯环的贡献增加和乙烯基的振动运动，血红蛋白构象会发生变化。在组氨酸（2850、2860 和 2900 cm –1 ）和赖氨酸（2880 和 2860 cm –1 ）残基的 CH 2 和 CH 3 基团的对称和不对称振动的贡献中还检测到了修饰。讨论了位于细胞亚膜区域和细胞质中的血红蛋白的氧结合机制。