Evidence map›Paper›PMID 39904585›Full record

ArticleBiochemistry2025

Redox-Guided DNA Scanning by the Dynamic Repair Enzyme Endonuclease III.

Ayaz Hassan, Filipe C D A Lima, Frank N Crespilho

Abstract read
In one paragraph

Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Ayaz HassanSão Carlos Institute of Chemistry, University of São Paulo (USP), São Carlos, SP 13566-590, Brazil.ORCID 0009-0000-7732-5717
Filipe C D A LimaFederal Institute of Education, Science, and Technology of São Paulo, Matão, SP15991-502, Brazil.ORCID 0000-0001-7062-5450
Frank N CrespilhoSão Carlos Institute of Chemistry, University of São Paulo (USP), São Carlos, SP 13566-590, Brazil.ORCID 0000-0003-4830-652X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endonuclease III (EndoIII), a key enzyme in the base excision repair (BER) pathway, contains a [4Fe4S] cluster that facilitates DNA repair through DNA-mediated charge transfer. Recent findings indicate that the redox state of this cluster influences EndoIII's binding affinity for DNA, modulating the enzyme's activity. In this study, we investigated the structural and electronic changes of the [4Fe4S] cluster upon binding to double-stranded DNA (dsDNA) using Fourier transform infrared spectroscopy, density functional theory calculations, and machine learning models. Our results reveal shifts in Fe-S bond vibrational modes, suggesting stabilization of the oxidized [4Fe4S] cluster in proximity to negatively charged DNA. A machine learning model, trained on the spectral features of the EndoIII/DNA complex, predicted the enzyme-DNA binding distance, providing further insights into the structural changes upon binding. We correlated the electrochemical stabilization potential of 150 mV in the [4Fe4S] cluster with the enzyme's DNA-binding properties, demonstrating how the cluster's redox state plays a crucial role in both structural stability and DNA repair.

Indexed as

Deoxyribonuclease (Pyrimidine Dimer)DNADNA RepairEscherichia coli ProteinsIron-Sulfur ProteinsOxidation-ReductionSpectroscopy, Fourier Transform InfraredDeoxyribonuclease (Pyrimidine Dimer)DNAEscherichia coli ProteinsIron-Sulfur Proteins

Identifiers

PMID39904585
PMCPMC11840932

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.