ArticleJournal of the American Chemical Society2013
Multiplexed electrochemistry of DNA-bound metalloproteins.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- High Affinity Aptamers and Their Specificity for Azaspiracid-2 Using Capture-SELEX.Marine drugs · 2025Article
- Modification of the 4Fe-4S Cluster Charge Transport Pathway Alters RNA Synthesis by Yeast DNA Primase.Biochemistry · 2022Article
- The [4Fe4S] Cluster of Yeast DNA Polymerase ε Is Redox Active and Can Undergo DNA-Mediated Signaling.Journal of the American Chemical Society · 2021Article
- Bottom-Up Fabrication of Plasmonic Nanoantenna-Based High-throughput Multiplexing Biosensors for Ultrasensitive Detection of microRNAs Directly from Cancer Patients' Plasma.Analytical chemistry · 2020Article
- UvrC Coordinates an OJournal of the American Chemical Society · 2020Article
- Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication.Annual review of biochemistry · 2019Review
- Substrate Binding Regulates Redox Signaling in Human DNA Primase.Journal of the American Chemical Society · 2018Article
- Nitric Oxide Modulates Endonuclease III Redox Activity by a 800 mV Negative Shift upon [FeJournal of the American Chemical Society · 2018Article
- A human MUTYH variant linking colonic polyposis to redox degradation of the [4Fe4S]Nature chemistry · 2018Article
- Sensing DNA through DNA Charge Transport.ACS chemical biology · 2018Review
- A Redox Role for the [4Fe4S] Cluster of Yeast DNA Polymerase δ.Journal of the American Chemical Society · 2017Article
- Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [FeJournal of the American Chemical Society · 2017Article
- Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.Science (New York, N.Y.) · 2017Article
- Electrical Probes of DNA-Binding Proteins.Methods in enzymology · 2017Article
- Redox Signaling through DNA.Israel journal of chemistry · 2016Article
- Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe-2S cluster.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Multiscattering-enhanced optical biosensor: multiplexed, non-invasive and continuous measurements of cellular processes.Biomedical optics express · 2015Article
- Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics.Chemical reviews · 2015Review
- DNA charge transport within the cell.Biochemistry · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Here we describe a multiplexed electrochemical characterization of DNA-bound proteins containing [4Fe-4S] clusters. DNA-modified electrodes have become an essential tool for the characterization of the redox chemistry of DNA repair proteins containing redox cofactors, and multiplexing offers a means to probe different complex samples and substrates in parallel to elucidate this chemistry. Multiplexed analysis of endonuclease III (EndoIII), a DNA repair protein containing a [4Fe-4S] cluster known to be accessible via DNA-mediated charge transport, shows subtle differences in the electrochemical behavior as a function of DNA morphology. The peak splitting, signal broadness, sensitivity to π-stack perturbations, and kinetics were all characterized for the DNA-bound reduction of EndoIII on both closely and loosely packed DNA films. DNA-bound EndoIII is seen to have two different electron transfer pathways for reduction, either through the DNA base stack or through direct surface reduction; closely packed DNA films, where the protein has limited surface accessibility, produce electrochemical signals reflecting electron transfer that is DNA-mediated. Multiplexing furthermore permits the comparison of the electrochemistry of EndoIII mutants, including a new family of mutations altering the electrostatics surrounding the [4Fe-4S] cluster. While little change in the midpoint potential was found for this family of mutants, significant variations in the efficiency of DNA-mediated electron transfer were apparent. On the basis of the stability of these proteins, examined by circular dichroism, we propose that the electron transfer pathway can be perturbed not only by the removal of aromatic residues but also through changes in solvation near the cluster.
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