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Article

Characterization of the redox activity and disulfide bond formation in apurinic/apyrimidinic endonuclease.

Biochemistry - 17 Jan 2012

Luo Meihua, Zhang Jun, He Hongzhen, Su Dian, Chen Qiujia, Gross Michael L, Kelley Mark R, Georgiadis Millie M

Abstract excerpt

Apurinic/apyrimidinic endonuclease (APE1) is an unusual nuclear redox factor in which the redox-active cysteines identified to date, C65 and C93, are surface inaccessible residues whose activities may be influenced by partial unfolding of APE1. To assess the role of the five remaining cysteines in APE1's redox activity, double-cysteine mutants were analyzed, excluding C65A, which is redox-inactive as a single...

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Identifiers

PMID: 22148505
DOI: 10.1021/bi201034z
PMCID: PMC3293223

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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