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首页> 外文期刊>The journal of physical chemistry, C. Nanomaterials and interfaces >Denaturation of cytochrome c and its peroxidase activity when immobilized on SAM films
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Denaturation of cytochrome c and its peroxidase activity when immobilized on SAM films

机译：固定在SAM膜上时细胞色素c的变性及其过氧化物酶活性

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This work uses cytochrome c, an electron carrier in the respiratory chain, as a model to probe how surface adsorption affects the folding of a protein. The electrochemical activities of the protein horse heart cytochrome c is studied under conditions where it is covalently attached onto a mixed carboxylic acid and hydroxyl-terminated SAM, which covers a Au electrode's surface. Changing the pH of the electrochemical buffer solution changes the conformation of the cytochrome c and causes a change of the peak currents in cyclic voltammetry and a shift of the peak potential. In addition, the unfolded cytochrome c displays peroxidase activity; the apparent Michaelis-Menten constant K-m for cytochrome c at these surfaces has been determined to be 7.9 mM at pH 3 and 144.3 mM at pH 7.
机译：这项工作使用细胞色素c（呼吸链中的电子载体）作为模型来探测表面吸附如何影响蛋白质的折叠。研究了蛋白质马心细胞色素c在共价键合到混合羧酸和羟基末端SAM（覆盖金电极表面）的条件下的电化学活性。改变电化学缓冲溶液的pH会改变细胞色素c的构象，并导致循环伏安法中峰电流的变化和峰电位的移动。另外，展开的细胞色素c显示出过氧化物酶活性。在这些表面上，细胞色素c的表观Michaelis-Menten常数K-m已确定在pH 3时为7.9 mM，在pH 7时为144.3 mM。

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