Abstract
We studied the effects of total and partial deuteration on the kinetics of thermal denaturation of met-hemoglobin. The kinetics were shown to be first order with respect to protein concentration: this was true both in H2O and in D2O within the entire range of temperatures examined. Deuterium oxide increased the stability of the native conformation of met-hemoglobin: this effect increased progressively by increasing the amount of D2O in the solution. Extension of the experiments to the amplest possible temperature range (50–63°C) allowed the determination of the isotopic effect on the activation enthalpy and entropy of the denaturation reaction; the isotopic effect resulted to be mainly entropic.
Our results do not support an interpretation in terms of purely steric effects due to the deuteration of the protein; rather, they suggest that solvent effects, possibly through protein-solvent hydrophobic interactions, are relevant.
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© 1980 Plenum Press, New York
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Cupane, A., Giacomazza, D., Madonia, F., San Biagio, P.L., Vitrano, E. (1980). Isotopic Effects on the Kinetics of Thermal Denaturation of Met-Hemoglobin. In: Borsellino, A., Omodeo, P., Strom, R., Vecli, A., Wanke, E. (eds) Developments in Biophysical Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1077-8_27
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DOI: https://doi.org/10.1007/978-1-4684-1077-8_27
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