Structural transformations of cytochrome c upon interaction with cardiolipin.
Structural transformations of cytochrome c upon interaction with cardiolipin.
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DOI：
10.1016/j.chemphyslip.2013.11.002
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发表时间：
2014-04
影响因子：
3.4
通讯作者：
Pletneva EV
中科院分区：
文献类型：
--
作者：
Muenzner J;Pletneva EV
细胞色素c（cyt c）与心磷脂（CL）的相互作用在细胞凋亡的早期阶段起着关键作用。在结合CL后，细胞色素c经历了二级和三级结构的变化，导致其过氧化物酶活性急剧增加。插入到膜的蛋白质，CL酰基链插入到蛋白质内部，和广泛展开的细胞色素C吸附到膜后已被提出作为可能的模式与CL的相互作用的细胞色素C。Met80的解离伴随着血红素裂隙的打开和另一个血红素配体的结合。荧光研究揭示了脂质结合蛋白质集合体的构象异质性，其具有不同的多肽构象，这些构象在蛋白质展开的程度上不同。我们将这些最新的研究结果与其他生物物理观测和合理化的实验条件中定义的构象特性和过氧化物酶活性的细胞色素c合奏的作用。最新的时间分辨研究提出了心磷脂诱导细胞色素c结构转变的触发和顺序。
Interactions of cytochrome c (cyt c) with cardiolipin (CL) play a critical role in early stages of apoptosis. Upon binding to CL, cyt c undergoes changes in secondary and tertiary structure that lead to a dramatic increase in its peroxidase activity. Insertion of the protein into membranes, insertion of CL acyl chains into the protein interior, and extensive unfolding of cyt c after adsorption to the membrane have been proposed as possible modes for interaction of cyt c with CL. Dissociation of Met80 is accompanied by opening of the heme crevice and binding of another heme ligand. Fluorescence studies have revealed conformational heterogeneity of the lipid-bound protein ensemble with distinct polypeptide conformations that vary in the degree of protein unfolding. We correlate these recent findings to other biophysical observations and rationalize the role of experimental conditions in defining conformational properties and peroxidase activity of the cyt c ensemble. Latest time-resolved studies propose the trigger and the sequence of cardiolipin-induced structural transitions of cyt c.
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