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Article

Quaternary structure influences the peroxidase activity of peroxiredoxin 3.

Biochemical and biophysical research communications - 4 Mar 2018

Yewdall N Amy, Peskin Alexander V, Hampton Mark B, Goldstone David C, Pearce F Grant, Gerrard Juliet A

Abstract excerpt

Peroxiredoxins are abundant peroxidase enzymes that are key regulators of the cellular redox environment. A major subgroup of these proteins, the typical 2-Cys peroxiredoxins, can switch between dimers and decameric or dodecameric rings, during the catalytic cycle. The necessity of this change in quaternary structure for function as a peroxidase is not fully understood. In order to explore this, human...

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PMID: 29438714
DOI: 10.1016/j.bbrc.2018.02.093

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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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