Saroff Harry A
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Biopolymers. 2007;85(5-6):450-5. doi: 10.1002/bip.20652.
Analyses of the binding of oxygen to monomers such as myoglobin employ the Mass Action equation. The Mass Action equation, as such, is not directly applicable for the analysis of the binding of oxygen to oligomers such as hemoglobin. When the binding of oxygen to hemoglobin is analyzed, models incorporating extensions of mass action are employed. Oxidation-reduction reactions of the heme group in myoglobin and hemoglobin involve the binding and dissociation of electrons. This reaction is described with the Nernst equation. The Nernst equation is applicable only to a monomeric species even if the number of electrons involved is greater than unity. To analyze the oxidation-reduction reaction in a molecule such as hemoglobin a model is required which incorporates extensions of the Nernst equation. This communication develops models employing the Nernst equation for oxidation-reduction reactions analogous to those employed for hemoglobin in the analysis of the oxygenation (binding of oxygen) reaction.
对诸如肌红蛋白等单体与氧气结合的分析采用质量作用方程。然而,质量作用方程本身并不直接适用于分析诸如血红蛋白等寡聚体与氧气的结合。在分析血红蛋白与氧气的结合时,会采用包含质量作用扩展的模型。肌红蛋白和血红蛋白中血红素基团的氧化还原反应涉及电子的结合和解离。此反应可用能斯特方程来描述。即使所涉及的电子数大于1,能斯特方程也仅适用于单体物种。为了分析诸如血红蛋白等分子中的氧化还原反应,需要一个包含能斯特方程扩展的模型。本文建立了一些模型,这些模型在分析氧合(氧气结合)反应时采用能斯特方程来处理类似于血红蛋白中的氧化还原反应。