[Kinetics of the reaction between hemoglobin and carbon monoxide. III. Existence of conformationally unequal Hb molecules during the process of CO binding and dissociation].
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.
D002248:Carbon Monoxide; D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins; D007700:Kinetics; D008968:Molecular Conformation
D006454:Hemoglobins; D002248:Carbon Monoxide
Kinetika reaktsii gemoglobina s okis'iu ugleroda. III. O sushchestvovanii konformatsionno-neravnovesnykh molekul Hb v protesessakh prisoedineniia i dissotsiatsii CO