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Article

Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4.

The Biochemical journal - 15 Mar 2011

Bjørnstad Linn G, Zoppellaro Giorgio, Tomter Ane B, Falnes Pål Ø, Andersson K Kristoffer

Abstract excerpt

The Fe(II)/2OG (2-oxoglutarate)-dependent dioxygenase superfamily comprises proteins that couple substrate oxidation to decarboxylation of 2OG to succinate. A member of this class of mononuclear non-haem Fe proteins is the Escherichia coli DNA/RNA repair enzyme AlkB. In the present work, we describe the magnetic and optical properties of the yet uncharacterized human ALKBH4 (AlkB homologue). Through EPR and...

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Identifiers

PMID: 21166655
DOI: 10.1042/BJ20101667
PMCID: PMC3048578

Genes

ALKBH4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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