Bliumenfel'd L A, Ermakov Iu A, Pasechnik V I
Biofizika. 1977 Jan-Feb;22(1):8-14.
The experimental data concerning CO binding to Hb in linear kinetic experiments were compared with theoretical results obtained earlier for several models. The results indicate that during the processes of CO binding and dissociation there appears Hb and HbCO molecules in out-or equilibrium conformational states. The dissociation effective rate constants for these HbCO molecules, formed from Hb molecules in equilibrium conformational state are kdiss greater than or equal to 5.5 s-1. At the same time, the equilibrium HbCO complexes after conformational relaxation have much smaller values of kdiss near to the well known literature values, i.e. 0.015 s-1.
将线性动力学实验中有关一氧化碳与血红蛋白结合的实验数据，与先前针对几种模型获得的理论结果进行了比较。结果表明，在一氧化碳结合和解离过程中，会出现处于非平衡或平衡构象状态的血红蛋白和碳氧血红蛋白分子。由处于平衡构象状态的血红蛋白分子形成的这些碳氧血红蛋白分子的解离有效速率常数kdiss大于或等于5.5 s-1。同时，构象弛豫后的平衡碳氧血红蛋白复合物的kdiss值要小得多，接近众所周知的文献值，即0.015 s-1。
