THERMODYNAMIC ANALYSIS OF CARBON-MONOXIDE BINDING BY HEMOGLOBIN TROUT-I
THERMODYNAMIC ANALYSIS OF CARBON-MONOXIDE BINDING BY HEMOGLOBIN TROUT-I
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DOI:
10.1016/0301-4622(79)85006-1
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发表时间:
1979-01-01
影响因子:
3.8
通讯作者:
GILL, SJ
中科院分区:
文献类型:
--
作者:
BARISAS, BG;GILL, SJ
Calorimetric measurements at 25.degree. C of the differential heat of CO binding by Hb trout I were examined together with the CO binding isotherms for the protein at 4.degree. C and 20.degree. C. Simultaneous treatment of these data sets by a statistically rigorous technique permitted evaluation of all the thermodynamic parameters for both the Adair and the Monod, Wyman, Changeux (MWC) models. The unusual temperature dependent cooperativity which this Hb exhibits were shown. In the Adair formalism the increasingly favorable free energy change for successive steps of ligand binding were nearly linearly paralleled by increasingly negative enthalpy changes for these steps. This caused the enhanced cooperativity observed as the temperature was decreased. For the MWC case, lowering the temperature increased the stability of the unligated T state relative to the unligated R state since the enthalpy of the T .fwdarw. R transition was 29.4 kcal mol-1. Simultaneously, the favorability of ligating R forms relative to T was enhanced since R form ligation was 14.1 kcal (mol CO)-1 more exothermic than that of T. The balance between these opposing effects was to increase ligand binding cooperativity at low temperatures. The predicted temperature dependence of the Hill coefficient for the MWC and Adair models was identical at low and intermediate temperatures but, interestingly, would show a strong divergence at high temperatures where negative cooperativity is suggested for the Adair case and positive cooperativity for the MWC case.