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Response to Comments on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”
Science ( IF 56.9 ) Pub Date : 2017-07-20 , DOI: 10.1126/science.aan2762
Elizabeth O’Brien 1 , Marilyn E. Holt 2 , Matthew K. Thompson 2 , Lauren E. Salay 2 , Aaron C. Ehlinger 2 , Walter J. Chazin 2 , Jacqueline K. Barton 1
Affiliation  

Baranovskiy et al. and Pellegrini argue that, based on structural data, the path for charge transfer through the [4Fe4S] domain of primase is not feasible. Our manuscript presents electrochemical data directly showing charge transport through DNA to the [4Fe4S] cluster of a primase p58C construct and a reversible switch in the DNA-bound signal with oxidation/reduction, which is inhibited by mutation of three tyrosine residues. Although the dispositions of tyrosines differ in different constructs, all are within range for microsecond electron transfer.

中文翻译:

对“[4Fe4S] 人类 DNA 引物酶簇作为使用 DNA 电荷传输的氧化还原开关”的评论的回应

巴拉诺夫斯基等人。和 Pellegrini 认为,根据结构数据,电荷转移通过 primase 的 [4Fe4S] 域的路径是不可行的。我们的手稿提供了电化学数据,直接显示电荷通过 DNA 传输到引物酶 p58C 构建体的 [4Fe4S] 簇,以及 DNA 结合信号的可逆转换与氧化/还原,这受到三个酪氨酸残基突变的抑制。尽管酪氨酸的配置在不同的结构中有所不同,但都在微秒电子转移的范围内。
更新日期:2017-07-20
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