The FeoC [4Fe–4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive
نویسندگان
چکیده
منابع مشابه
Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA.
Escherichia coli endonuclease III (EndoIII) and MutY are DNA glycosylases that contain [4Fe4S] clusters and that serve to maintain the integrity of the genome after oxidative stress. Electrochemical studies on highly oriented pyrolytic graphite (HOPG) revealed that DNA binding by EndoIII leads to a large negative shift in the midpoint potential of the cluster, consistent with stabilization of t...
متن کاملThe [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.
DNA charge transport chemistry offers a means of long-range, rapid redox signaling. We demonstrate that the [4Fe4S] cluster in human DNA primase can make use of this chemistry to coordinate the first steps of DNA synthesis. Using DNA electrochemistry, we found that a change in oxidation state of the [4Fe4S] cluster acts as a switch for DNA binding. Single-atom mutations that inhibit this charge...
متن کاملResponse to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
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 muta...
متن کاملComment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
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.
متن کاملFeoC from Klebsiella pneumoniae contains a [4Fe-4S] cluster.
Iron is essential for pathogen survival, virulence, and colonization. Feo is suggested to function as the ferrous iron (Fe(2+)) transporter. The enterobacterial Feo system is composed of 3 proteins: FeoB is the indispensable component and is a large membrane protein likely to function as a permease; FeoA is a small Src homology 3 (SH3) domain protein that interacts with FeoB; FeoC is a winged-h...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2019
ISSN: 0006-2960,1520-4995
DOI: 10.1021/acs.biochem.9b00745