Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport"
- PMID: 28729486
- DOI: 10.1126/science.aan2954
Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport"
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.
Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
Comment in
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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. Science. 2017. PMID: 28729485 Free PMC article.
Comment on
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The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.Science. 2017 Feb 24;355(6327):eaag1789. doi: 10.1126/science.aag1789. Science. 2017. PMID: 28232525 Free PMC article.
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