Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".

Elizabeth O'Brien, Marilyn E Holt, Matthew K Thompson, Lauren E Salay, Aaron C Ehlinger, Walter J Chazin, Jacqueline K Barton

Science (New York, N.Y.) 2017 Jul 21

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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. Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.

Citation

Elizabeth O'Brien, Marilyn E Holt, Matthew K Thompson, Lauren E Salay, Aaron C Ehlinger, Walter J Chazin, Jacqueline K Barton. Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport". Science (New York, N.Y.). 2017 Jul 21;357(6348)