DNA repair glycosylases with a [4Fe-4S] cluster: A redox cofactor for DNA-mediated charge transport?
DNA repair glycosylases with a [4Fe-4S] cluster: A redox cofactor for DNA-mediated charge transport?
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DOI：
10.1016/j.jinorgbio.2007.05.001
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发表时间：
2007-11-01
影响因子：
3.9
通讯作者：
Barton, Jacqueline K.
中科院分区：
文献类型：
--
作者：
Boal, Amie K.;Yavin, Eylon;Barton, Jacqueline K.
[4Fe-4S]簇普遍存在于从细菌到人类的生物体中的一类碱基切除修复酶中，并且由于其在生理条件下的氧化还原稳定性而首先被认为是一种结构元素。当研究与 DNA 结合时，其中两种修复蛋白（来自大肠杆菌的 MutY 和核酸内切酶 III）表现出 DNA 依赖性可逆电子转移，具有高电位铁蛋白的典型特征。这些结果激发了人们重新审视 [4Fe-4S] 簇在此类酶中的作用。 [4Fe-4S] 簇是否可以用作氧化还原辅助因子，利用 DNA 介导的电荷传输（众所周知，该过程对损伤和错配碱基高度敏感）来搜索受损位点？这里描述的实验证明了 DNA 介导的电荷传输在表征这些 DNA 结合金属蛋白方面的效用，以及阐明 DNA 作为蛋白质之间的电子信号介质的这种新功能的努力。 (c) 2007 Elsevier Inc. 保留所有权利。
The [4Fe-4S] cluster is ubiquitous to a class of base excision repair enzymes in organisms ranging from bacteria to man and was first considered as a structural element, owing to its redox stability under physiological conditions. When studied bound to DNA, two of these repair proteins (MutY and Endonuclease III from Escherichia coli) display DNA-dependent reversible electron transfer with characteristics typical of high potential iron proteins. These results have inspired a reexamination of the role of the [4Fe-4S] cluster in this class of enzymes. Might the [4Fe-4S] cluster be used as a redox cofactor to search for damaged sites using DNA-mediated charge transport, a process well known to be highly sensitive to lesions and mismatched bases? Described here are experiments demonstrating the utility of DNA-mediated charge transport in characterizing these DNA-binding metalloproteins, as well as efforts to elucidate this new function for DNA as an electronic signaling medium among the proteins. (c) 2007 Elsevier Inc. All rights reserved.