Cytochrome c: a thermodynamic study of the relationship among oxidation state, ion-binding and structural parameters. Cation binding to horse-heart ferrocytochrome c.
Cytochrome c: a thermodynamic study of the relationship among oxidation state, ion-binding and structural parameters. Cation binding to horse-heart ferrocytochrome c.
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细胞色素 c：氧化态、离子结合和结构参数之间关系的热力学研究。
DOI：
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发表时间：
1974
期刊：
影响因子：
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通讯作者：
A. Schejter
中科院分区：
文献类型：
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作者：
R. Margalit;A. Schejter
用凝胶过滤法研究了阳离子与马心铁细胞色素c的特异性结合。研究的阳离子是：Mg 2+，Co 2+，辛可宁和原黄素。稳定常数在5-8 mM-1的范围内，每个蛋白质分子的结合位点数为1 - 2。测定了Mg ~（2+）-亚铁细胞色素体系的稳定常数随温度的变化关系。热力学参数为：Δ H 0 obs =+ 12 kcal/mol，Δ G 0 obs，（25°C）=−5.6 kcal/mol，Δ S 0 obs =+ 57 cal × mob 1 × K−1。
The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5–8 mM−1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+-ferrocytochrome system was measured. The thermodynamic parameters were found to be: ΔH0obs=+ 12 kcal/mol, ΔG0obs, (25°C) =−5.6 kcal/mol and ΔS0obs=+ 57 cal × mob1× K−1.