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

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.

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Publication Details

Journal
Biochemistry
Published
2025-02-04
DOI
https://doi.org/10.1021/acs.biochem.4c00621
Primary Topic
Advanced biosensing and bioanalysis techniques
Type
article
Field-Weighted Citation Impact
0.00

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article

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

Ayaz Hassan, Filipe C. D. A. Lima, Frank N. Crespilho
Biochemistry
Advanced biosensing and bioanalysis techniques
article

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

Ayaz Hassan, Filipe C. D. A. Lima, Frank N. Crespilho
article en

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.

BiochemistryVol. 64(4)
Federal Institute of São Paulo (BR), COMSATS University Islamabad (PK), Hospital Universitário da Universidade de São Paulo (BR)
Ministry of Science and Technology, Pakistan, Fundação de Amparo à Pesquisa do Estado de São Paulo, Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico
Openalex Percentile: Top 98%
Advanced biosensing and bioanalysis techniques
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Redox-Guided DNA Scanning by the Dynamic Repair Enzyme Endonuclease III — Ayaz Hassan, Filipe C. D. A. Lima, et al. · Biochemistry (2025) | TGRS Research Map | TGRS