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.
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