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An extended Monod-Wyman-Changeaux-model expressed in terms of the Herzfeld-Stanley formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV
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An extended Monod-Wyman-Changeaux-model expressed in terms of the Herzfeld-Stanley formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV

R Schweitzer-Stenner and W Dreybrodt
Biophysical journal, v 55(4), pp 691-701
Apr 1989
PMID: 2720067
url
https://doi.org/10.1016/s0006-3495(89)82868-1View
Published, Version of Record (VoR)Open Access (Publisher-Specific) Open
url
https://doi.org/10.1016/S0006-3495(89)82868-1View
Published, Version of Record (VoR) Open

Abstract

Animals Carbon Monoxide - blood Carboxyhemoglobin - metabolism Hemoglobins - metabolism Kinetics Ligands Mathematics Models, Theoretical Oxygen - blood Oxyhemoglobins - metabolism Protein Binding Protein Conformation Thermodynamics Trout
An extended Monod, Wyman, Changeaux (MWC)-model, the mathematical basis of which had been formulated by Herzfeld and Stanley (J. Mol. Blol. 82:231. 1974.) was used to fit oxygen and CO-binding curves of hemoglobin trout IV measured at different pH-values between pH = 8.0 and 6.0. From this calculation one obtains that even the fully liganded molecule exhibits a R---T quaternary transition upon approaching the acid pH-region. In the case of O2-binding, the cooperativity becomes negative below pH = 6.5. This can be related to the difference between the equilibrium constants of proton binding to the alpha- and beta-subunits. Furthermore, it can be shown that the interaction between the quaternary T---R- and the tertiary t---r-transitions is different for the alpha- and beta-subunits.

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Biophysics
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