RRC ID 35242
Author Létoffé S, Heuck G, Delepelaire P, Lange N, Wandersman C.
Title Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact.
Journal Proc Natl Acad Sci U S A
Abstract Because heme is a major iron-containing molecule in vertebrates, the ability to use heme-bound iron is a determining factor in successful infection by bacterial pathogens. Until today, all known enzymes performing iron extraction from heme did so through the rupture of the tetrapyrrol skeleton. Here, we identified 2 Escherichia coli paralogs, YfeX and EfeB, without any previously known physiological functions. YfeX and EfeB promote iron extraction from heme preserving the tetrapyrrol ring intact. This novel enzymatic reaction corresponds to the deferrochelation of the heme. YfeX and EfeB are the sole proteins able to provide iron from exogenous heme sources to E. coli. YfeX is located in the cytoplasm. EfeB is periplasmic and enables iron extraction from heme in the periplasm and iron uptake in the absence of any heme permease. YfeX and EfeB are widespread and highly conserved in bacteria. We propose that their physiological function is to retrieve iron from heme.
Volume 106(28)
Pages 11719-24
Published 2009-7-14
DOI 10.1073/pnas.0903842106
PII 0903842106
PMID 19564607
PMC PMC2710666
MeSH Cation Transport Proteins / metabolism* Chromatography, High Pressure Liquid Escherichia coli / metabolism* Escherichia coli Proteins / metabolism* Heme / chemistry* Iron / chemistry Iron / metabolism* Iron-Binding Proteins / metabolism* Mass Spectrometry Protein Binding Protoporphyrins / metabolism Tetrapyrroles / chemistry
IF 9.412
Times Cited 104
Prokaryotes E. coli JW2424 JW1004