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Article

Spectroscopic studies of single and double variants of M ferritin: lack of conversion of a biferrous substrate site into a cofactor site for O2 activation.

Biochemistry - 28 Jan 2014

Kwak Yeonju, Schwartz Jennifer K, Haldar Suranjana, Behera Rabindra K, Tosha Takehiko, Theil Elizabeth C, Solomon Edward I

Abstract excerpt

Ferritin has a binuclear non-heme iron active site that functions to oxidize iron as a substrate for formation of an iron mineral core. Other enzymes of this class have tightly bound diiron cofactor sites that activate O2 to react with substrate. Ferritin has an active site ligand set with 1-His/...

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Identifiers

PMID: 24397299
DOI: 10.1021/bi4013726
PMCID: PMC3985457

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24397299-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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