Oxygen binding of arthropod hemocyanin The role of allosteric equilibria in terms of the nested Monod-Wyman-Changeux model

Abstract

When the oxygen binding of the hemocyanin from the lobsterHomarus americanus was analysed in terms of the nested Monod-Wyman-Changeux model, it revealed that protons affect the allosteric equilibria between four conformations. Applying computer simulations we have demonstrated the specific influence of the three different allosteric equilibrium constants on the affinity and cooperativity of oxygen binding.