Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”

Andrey G. Baranovskiy; Nigar D. Babayeva; Yinbo Zhang; Luis Blanco; Youri I. Pavlov; Tahir H. Tahirov

doi:10.1126/science.aan2396

Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”

Andrey G. Baranovskiy, Nigar D. Babayeva, Yinbo Zhang, Luis Blanco, Youri I. Pavlov, Tahir H. Tahirov

Research output: Contribution to journal › Comment/debate › peer-review

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Abstract

O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.

Original language	English (US)
Article number	eaan2396
Journal	Science
Volume	357
Issue number	6348
DOIs	https://doi.org/10.1126/science.aan2396
State	Published - Jul 21 2017

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title = "Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”",

abstract = "O{\textquoteright}Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.",

author = "Baranovskiy, {Andrey G.} and Babayeva, {Nigar D.} and Yinbo Zhang and Luis Blanco and Pavlov, {Youri I.} and Tahirov, {Tahir H.}",

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AU - Baranovskiy, Andrey G.

AU - Babayeva, Nigar D.

AU - Zhang, Yinbo

AU - Blanco, Luis

AU - Pavlov, Youri I.

AU - Tahirov, Tahir H.

PY - 2017/7/21

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N2 - O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.

AB - O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.

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Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”

Abstract

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