配体与高铁血红蛋白和高铁肌红蛋白结合时的体积变化。
Volume changes in binding of ligands to methemoglobin and metmyoglobin.
作者信息
Ogunmola G B, Kauzmann W, Zipp A
出版信息
Proc Natl Acad Sci U S A. 1976 Dec;73(12):4271-3. doi: 10.1073/pnas.73.12.4271.
The volume changes for the binding of various ligands to metmyoglobin and methemoglobin have been determined from the effect of pressure on the binding constants (for metmyoglobin) and by direct dilatometry (for methemoglobin). The volume changes associated with the binding of cyanide and azide ions to methemoglobin are pH-dependent. The volume change for the binding reaction is evidently affected by the same subtle structural variations that have been judged to be present from the variation with pH of enthalpy and entropy for the binding reactions in these proteins. Hydration changes and spin state changes which have been postulated to be linked with structural variations in these proteins must be pH-dependent.
已通过压力对结合常数的影响（针对高铁肌红蛋白）以及直接膨胀测量法（针对高铁血红蛋白）确定了各种配体与高铁肌红蛋白和高铁血红蛋白结合时的体积变化。与氰化物和叠氮离子与高铁血红蛋白结合相关的体积变化取决于pH值。结合反应的体积变化显然受到相同细微结构变化的影响，这些结构变化已从这些蛋白质结合反应的焓和熵随pH值的变化判断出来。假定与这些蛋白质结构变化相关的水合变化和自旋态变化一定取决于pH值。
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