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American Association for the Advancement of Science, Science, 6348(357), 2017

DOI: 10.1126/science.aan2954

American Association for the Advancement of Science, Science, 6348(357), 2017

DOI: 10.1126/science.aan2396

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Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”

Journal article published in 2017 by Andrey G. Baranovskiy ORCID, Yinbo Zhang ORCID, Tahir H. Tahirov ORCID, Nigar D. Babayeva, Luis Blanco ORCID, Youri I. Pavlov, Luca Pellegrini ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

O’Brien et al . (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 et al .