Department of Biochemistry, University of Cambridge, Cambridge, UK.
Science. 2017 Jul 21;357(6348). doi: 10.1126/science.aan2954.
O'Brien (Research Article, 24 February 2017, eaag1789) report that the iron-sulfur cluster of primase has a redox role in enzyme activity. Their analysis is based on a partially misfolded structure of the iron-sulfur cluster domain of primase. In the correctly folded structure, two of the three tyrosines putatively involved in electron transfer, Y345 and Y347, contact the RNA/DNA helix, providing an alternative explanation for the data of O'Brien .
奥布莱恩（Research Article，2017 年 2 月 24 日，eaag1789）报告称，引物酶的铁硫簇在酶活性中具有氧化还原作用。他们的分析基于引物酶的铁硫簇结构域的部分错误折叠结构。在正确折叠的结构中，三个假定参与电子转移的酪氨酸中的两个，Y345 和 Y347，与 RNA/DNA 螺旋接触，为奥布莱恩的数据提供了另一种解释。
