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

Science. 2017 Jul 21;357(6348):eaan2762. doi: 10.1126/science.aan2762.

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.

Publication types

  • Comment

MeSH terms

  • Biological Transport
  • DNA
  • DNA Primase / chemistry*
  • Electron Transport
  • Humans
  • Oxidation-Reduction*

Substances

  • DNA
  • DNA Primase