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Article

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.

The Journal of biological chemistry - 23 Jan 2015

Sea Kevin, Sohn Se Hui, Durazo Armando, Sheng Yuewei, Shaw Bryan F, Cao Xiaohang, Taylor Alexander B, Whitson Lisa J, Holloway Stephen P, Hart P John, Cabelli Diane E, Gralla Edith Butler, Valentine Joan Selverstone

Abstract excerpt

The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond. We determined x-ray crystal structures of metal-bound and metal-deficient hC57S SOD1. C57S hSOD1 isolated from yeast contained four zinc ions per protein dimer and was structurally very...

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Identifiers

PMID: 25433341
DOI: 10.1074/jbc.M114.588798
PMCID: PMC4303690

Genes

SOD1

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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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