Characterization of a partially unfolded high potential iron protein
Characterization of a partially unfolded high potential iron protein
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DOI：
10.1021/bi970810w
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发表时间：
1997-08-05
期刊：
影响因子：
2.9
通讯作者：
Piccioli, M
中科院分区：
文献类型：
--
作者：
Bertini, I;Cowan, JA;Piccioli, M
在向天然蛋白质中添加浓缩的氯化胍溶液后，来自 Chromatium vinosum 的含 Fe4S4 的高电位铁硫蛋白的部分未折叠状态已通过 NMR 光谱进行检测和表征。该中间物质（i）保持多金属中心，（ii）表现出很大程度上塌陷的二级结构，并且（iii）在氧化时经历东簇分解。该信息被纳入关于此类蛋白质的知识中，并且讨论了该中间体在体内折叠/解折叠过程中的可能作用以及其在氧化 HiPIP 的缓慢水解降解特征中的作用。
A partially unfolded state of the Fe4S4-containing high potential iron-sulfur protein from Chromatium vinosum has been detected and characterized by NMR spectroscopy following addition of a concentrated solution of guanidinium chloride to the native protein. This intermediate species (i) maintains the polymetallic center, (ii) exhibits a largely collapsed secondary structure, and (iii) undergoes East cluster decomposition upon oxidation. This information is framed into the knowledge about this class of proteins, and the possible role of this intermediate with respect to the in vivo folding/unfolding process is discussed as well its role in the slow hydrolytic degradation characteristic of oxidized HiPIPs.