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Experimental evidence suggests that DNA-mediated redox signaling between high-potential [Fe4S4] proteins is relevant to DNA replication and repair processes, and protein-mediated charge transfer (CT) between [Fe4S4] clusters and nucleic acids is a fundamental process of the signaling and repair mechanisms. We analyzed the dominant CT pathways in the base excision repair glycosylase MutY using molecular dynamics simulations and hole hopping pathway analysis. We find that the adenine nucleobase of the mismatched A·oxoG DNA base pair facilitates [Fe4S4]-DNA CT prior to adenine excision by MutY. We also find that the R153L mutation in MutY (linked to colorectal adenomatous polyposis) influences the dominant [Fe4S4]-DNA CT pathways and appreciably decreases their effective CT rates.


Ruijie D Teo, Xiaochen Du, Héctor Luis Torres Vera, Agostino Migliore, David N Beratan. Correlation between Charge Transport and Base Excision Repair in the MutY-DNA Glycosylase. The journal of physical chemistry. B. 2021 Jan 14;125(1):17-23

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PMID: 33371674

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