Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, USA
Review Article
Rate and Equilibrium Constants of O2-Binding and O2 Release: ?The Forward and Reverse Steps for the TState ? RState Change for Human Hb4/BPG, Under Standard Conditions?
Author(s): Francis Knowles*, Samantha Doyle and Douglas Magde
Three unknown quantities describe the O2-equilibrium binding curve for fractional saturation of human
hemoglobin in red blood cells, under standard conditions: Kα, the O2-binding constant of equivalent Tstate
α-chains; KΔ, the equilibrium constant for the Tstate → Rstate transition; Kβ, the O2-binding constant of
equivalent Rstate β-chains. The model for formulation of the equation of state is a 3-stage ordered sequence of
reactions.
Values of Kα, KΔ and Kβ were established by determination of rate constants for the oxyg.. View more»