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首页> 外文期刊>Biochemistry >Peroxidase Activity as a Tool for Studying the Folding of c-Type Cytochromes.
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Peroxidase Activity as a Tool for Studying the Folding of c-Type Cytochromes.

机译：过氧化物酶活性作为研究折叠c型细胞色素的工具。

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摘要

The peroxidase activity of c-type cytochromes increases substantially by unfolding. This phenomenon was used to study the equilibrium unfolding of ferricytochrome c. The peroxidase activity is already enhanced at low denaturant concentrations. The lowest free energy folding intermediate is easily detected by this method, while it is invisible using fluorescence or optical spectroscopy. The free energy difference between this folding intermediate and the native state depends on the strength of the sixth ligand of the heme-iron and the increase in peroxidase activity upon unfolding is shown to be a sensitive indicator of the strength of this ligand. Under fully denaturing conditions, the peroxidase activity is inhibited by protein-based ligands. It is shown that at least three different ligand groups can be responsible for this inhibition, and that at neutral or alkaline pH, the predominant ligand is not histidine. The use of peroxidase activity assays as a method to study the unfolding of cytochrome c is evaluated.
机译：通过展开，c型细胞色素的过氧化物酶活性大大提高。该现象用于研究亚铁色素c的平衡展开。在低变性剂浓度下，过氧化物酶活性已经增强。最低的自由能折叠中间体很容易通过这种方法检测，而使用荧光或光谱学则看不见。该折叠中间体与天然状态之间的自由能差取决于血红素铁的第六个配体的强度，并且在展开时过氧化物酶活性的增加被证明是该配体强度的敏感指标。在完全变性的条件下，过氧化物酶活性被基于蛋白质的配体抑制。已显示至少三个不同的配体基团可导致这种抑制，并且在中性或碱性pH下，主要的配体不是组氨酸。评价了过氧化物酶活性测定法作为研究细胞色素c的展开的方法。

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