Ascoli F, Gratton E, Riva F, Fasella P, Brunori M
Biochim Biophys Acta. 1978 Apr 26;533(2):534-7. doi: 10.1016/0005-2795(78)90400-2.
The infrared spectra of the carbomonoxy derivatives of the hemoglobin components I and IV from trout have been measured in the CO stretching frequency region using a high resolution infrared spectrometer. The CO stretching frequency of Hb I CO is very close to that of carbomonoxy human hemoglobin and is pH-independent. In contrast, the CO stretching frequency of Hb IV CO is higher and shows a small but significant pH dependence in the range 6.2-7.8. These results point to a decreased strength of the iron-CO bond in Hb IV CO at low pH, in agreement with the conclusions drawn from the reported difference spectra of Hb IV CO as a function of pH.
利用高分辨率红外光谱仪，在一氧化碳伸缩频率区域测量了虹鳟血红蛋白组分I和IV的碳氧单氧基衍生物的红外光谱。血红蛋白I碳氧单氧基（Hb I CO）的一氧化碳伸缩频率与碳氧单氧基人血红蛋白的非常接近，且与pH无关。相比之下，血红蛋白IV碳氧单氧基（Hb IV CO）的一氧化碳伸缩频率较高，并且在6.2 - 7.8范围内显示出微小但显著的pH依赖性。这些结果表明，在低pH值下，Hb IV CO中铁 - 一氧化碳键的强度降低，这与根据报道的Hb IV CO随pH变化的差示光谱得出的结论一致。
