Redox Signaling in Eukaryotic DNA Replication and Repair
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![Figure 1.1. The potential of the [4Fe4S] cluster cofactor is tunable over a wide range of physiological redox potential values](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/24.612.83.528.79.331/figure-potential-cluster-cofactor-tunable-physiological-potential-values.webp)
![Figure 1.2. [4Fe4S] cluster biogenesis and loading into client prokaryotic (above) and eukaryotic (below) proteins](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/26.612.78.547.361.619/figure-cluster-biogenesis-loading-client-prokaryotic-eukaryotic-proteins.webp)
![Table 1.1. DNA-processing, [4Fe4S] enzymes are found in all three domains of life (prokaryotes, archaea, and eukaryotes)](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/29.612.71.547.67.542/table-dna-processing-enzymes-domains-prokaryotes-archaea-eukaryotes.webp)
![Figure 1.5. Electrochemical methods to measure the redox potential of DNA-bound (top) and DNA-free (below) [4Fe4S] enzymes](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/36.612.122.499.68.318/figure-electrochemical-methods-measure-redox-potential-bound-enzymes.webp)
![Figure 1.6. DNA binding shifts the potential of [4Fe4S] cluster enzymes. Endonuclease III (above, left) has a redox potential of approximately 80mV vs](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/41.612.84.537.82.322/figure-binding-potential-cluster-enzymes-endonuclease-potential-approximately.webp)
![Figure 1.7. A model for DNA-mediated redox signaling between repair proteins. Enzymes with the cluster in the native [4Fe4S]2+ first bind DNA, causing the cluster to become activated toward oxidation](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/48.612.108.540.76.328/mediated-signaling-proteins-enzymes-causing-cluster-activated-oxidation.webp)
![Figure 1.10. Model for primase-polymerase α handoff through redox switching. A) Oxidized [4Fe4S]3+ primase is bound to the RNA/DNA primer during primer synthesis](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/60.612.177.453.75.569/figure-primase-polymerase-handoff-switching-oxidized-primase-synthesis.webp)
![Figure 1.11. [4Fe4S] enzymes in eukaryotic repair and replication. B-family polymerases, DNA primase, Dna2 helicase-nuclease, BER/NER enzymes such as MUTYH, NTHL1, and XPD, all coordinate a [4Fe4S] cluster cofactor](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/64.612.74.566.77.334/figure-eukaryotic-replication-polymerases-helicase-nuclease-coordinate-cofactor.webp)
![Fig. 2.1. Oxidized [4Fe4S]3+ and reduced [4Fe4S]2+ p58C display different behavior on DNA-modified electrodes](https://thumb-us.123doks.com/thumbv2/123dok_us/1118640.1141077/79.612.86.509.78.398/fig-oxidized-reduced-display-different-behavior-modified-electrodes.webp)
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