Published July 20, 2017
| Accepted Version
Journal Article
Open
Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport"
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.
Additional Information
© 2017 American Association for the Advancement of Science. 10 April 2017; accepted 13 June 2017.Attached Files
Accepted Version - nihms947704.pdf
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Additional details
- PMCID
- PMC5935490
- Eprint ID
- 79253
- DOI
- 10.1126/science.aan2762
- Resolver ID
- CaltechAUTHORS:20170720-130038340
- Created
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2017-07-20Created from EPrint's datestamp field
- Updated
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2022-03-23Created from EPrint's last_modified field