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Temperature dependence of the effects of some monohydric alcohols on the oxygen affinity of hemoglobin: Determination and analysis of thermodynamic parameters

✍ Scribed by Lorenzo Cordone; Antonio Cupane; Pier L. San Biagio; Eugenio Vitrano

Publisher: Wiley (John Wiley & Sons)
Year: 1981
Tongue: English
Weight: 527 KB
Volume: 20
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.1981.360200105

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✦ Synopsis

Abstract

We studied the effects of methanol, ethanol, iso‐propanol, and n‐propanol on the reaction of hemoglobin with oxygen at various temperatures. The analysis of the results in terms of the Monod‐Wyman‐Changeux model allowed determination of the overall contribution of the alcohols to the standard enthalpy and entropy differences between the T and R states of hemoglobin. A phenomenological approach allowed us to obtain separately the contributions related to the variations of the bulk dielectric constant of the solvent (bulk electrostatic contributions) and the contributions related to other effects (non‐bulk‐electrostatic contributions). The values of non‐bulk‐electrostatic contributions to ΔΔ__H__ and ΔΔ__S__ supported the suggestion that these contributions are mainly related to protein‐solvent hydrophobic interactions.

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