| Literature DB >> 28729485 |
Elizabeth O'Brien1, Marilyn E Holt2, Matthew K Thompson2, Lauren E Salay2, Aaron C Ehlinger2, Walter J Chazin3, Jacqueline K Barton4.
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.Entities:
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Year: 2017 PMID: 28729485 PMCID: PMC5935490 DOI: 10.1126/science.aan2762
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728