論文 - 詳細
| RRC ID | 35242 |
|---|---|
| 著者 | Létoffé S, Heuck G, Delepelaire P, Lange N, Wandersman C. |
| タイトル | Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact. |
| ジャーナル | 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. |
| 巻・号 | 106(28) |
| ページ | 11719-24 |
| 公開日 | 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 |
| 引用数 | 104 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 4 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 原核生物(大腸菌) | JW2424 JW1004 |