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Article

Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines.

The Journal of biological chemistry - 12 Aug 2005

Layer Gunhild, Grage Katrin, Teschner Thomas, Schünemann Volker, Breckau Daniela, Masoumi Ava, Jahn Martina, Heathcote Peter, Trautwein Alfred X, Jahn Dieter

Abstract excerpt

The S-adenosylmethionine (AdoMet) radical enzyme oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX during bacterial heme biosynthesis. The recently solved crystal structure of Escherichia coli HemN revealed the presence of an unusually coordinated iron-sulfur cluster and two molecules of AdoMet. EPR spectroscopy of the...

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PMID: 15967800
DOI: 10.1074/jbc.M501275200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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