Krishna Y V, Aruna B, Narayana P A
School of Physics, University of Hyderabad, India.
Biochim Biophys Acta. 1987 Nov 5;916(1):48-53. doi: 10.1016/0167-4838(87)90209-3.
Electron spin echo envelope modulation studies are performed on human hemoglobin cyanide, hemoglobin nitroxide and hemoglobin nitroxide + inositol hexaphosphate at neutral pH. The modulation data are Fourier transformed and are analyzed in the frequency domain. The frequency components observed from hemoglobin cyanide indicate modulation from the coordinated nitrogen N-1 of the proximal imidazole (His-F8). In the case of hemoglobin nitroxide, the binding of inositol hexaphosphate causes the nitrogen N-3 of the proximal imidazole to be protonated in some of the subunits. From a comparison with other studies on these derivatives of hemoglobin, these subunits are identified as the alpha-subunits.
在中性pH条件下，对人氰化血红蛋白、亚硝基血红蛋白以及亚硝基血红蛋白+肌醇六磷酸进行了电子自旋回波包络调制研究。调制数据进行傅里叶变换并在频域中进行分析。从氰化血红蛋白观察到的频率成分表明来自近端咪唑（His-F8）配位氮N-1的调制。在亚硝基血红蛋白的情况下，肌醇六磷酸的结合导致一些亚基中近端咪唑的氮N-3被质子化。通过与这些血红蛋白衍生物的其他研究进行比较，这些亚基被鉴定为α-亚基。
