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Article

Heme-responsive DNA binding by the global iron regulator Irr from Rhizobium leguminosarum.

The Journal of biological chemistry - 21 May 2010

Singleton Chloe, White Gaye F, Todd Jonathan D, Marritt Sophie J, Cheesman Myles R, Johnston Andrew W B, Le Brun Nick E

Abstract excerpt

Heme, a physiologically crucial form of iron, is a cofactor for a very wide range of proteins and enzymes. These include DNA regulatory proteins in which heme is a sensor to which an analyte molecule binds, effecting a change in the DNA binding affinity of the regulator. Given that heme, and more generally iron, must be carefully regulated, it is surprising that there are no examples yet in bacteria in which heme...

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Identifiers

PMID: 20233710
DOI: 10.1074/jbc.M109.067215
PMCID: PMC2871471

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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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