Published July 20, 2017 | Accepted Version
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Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport"

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Abstract

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.

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© 2017 American Association for the Advancement of Science. 10 April 2017; accepted 13 June 2017.

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