Effects of interface mutations on association modes and electron-transfer rates between proteins
Effects of interface mutations on association modes and electron-transfer rates between proteins
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DOI：
10.1073/pnas.0505176102
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发表时间：
2005-10-25
影响因子：
11.1
通讯作者：
Crane, BR
中科院分区：
文献类型：
--
作者：
Kang, SA;Crane, BR
虽然键合网络决定蛋白质内的电子转移（ET）速率，但结构和动力学影响蛋白质界面ET的机制还不清楚。光化学诱导的ET和随后的电荷之间的重组Zn-卟啉取代的细胞色素c过氧化物酶和细胞色素c在单晶体的测量与确定的结构的氧化还原合作伙伴的不同关联模式的反应性。晶体中的结构和ET速率与色氨酸氧化介导的电荷复合反应一致。界面上的保守突变可以极大地影响蛋白质的取向和处理氧化还原中心的方式。而一些配置是ET无活性的，野生型复合物表现出最快的重组速率。其他关联模式生成的ET率与基于辅因子分离或简单键合途径的预测不相关。光诱导ET的抑制
Although bonding networks determine electron-transfer (ET) rates within proteins, the mechanism by which structure and dynamics influence ET across protein interfaces is not well understood. Measurements of photochemically induced ET and subsequent charge recombination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single crystals correlate reactivity with defined structures for different association modes of the redox partners. Structures and ET rates in crystals are consistent with tryptophan oxidation mediating charge recombination reactions. Conservative mutations at the interface can drastically affect how the proteins orient and dispose redox centers. Whereas some configurations are ET inactive, the wild-type complex exhibits the fastest recombination rate. Other association modes generate ET rates that do not correlate with predictions based on cofactor separations or simple bonding pathways. Inhibition of photoinduced ET at