2008
DOI: 10.1002/iub.123
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Is the host heme incorporated in microbial heme‐proteins?

Abstract: [No abstract available

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Cited by 8 publications
(5 citation statements)
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“…Once internalized, iron and heme follow specific fates, balancing the nutritional needs with storage and preservation of the bacterium from potential toxicity. Hemic iron can be released by IsdG or IsdI through their oxygenase activity or, based on the "heme hijacking hypothesis", the heme acquired from the host can be exploited as a cofactor in the bacterial heme-proteins, for example in cytochromes [53,173,174]. This process could possibly be energetically favorable to S. aureus, explaining its preference for heme as an iron source.…”
Section: Heme and Iron Homeostasis Inside S Aureusmentioning
confidence: 99%
“…Once internalized, iron and heme follow specific fates, balancing the nutritional needs with storage and preservation of the bacterium from potential toxicity. Hemic iron can be released by IsdG or IsdI through their oxygenase activity or, based on the "heme hijacking hypothesis", the heme acquired from the host can be exploited as a cofactor in the bacterial heme-proteins, for example in cytochromes [53,173,174]. This process could possibly be energetically favorable to S. aureus, explaining its preference for heme as an iron source.…”
Section: Heme and Iron Homeostasis Inside S Aureusmentioning
confidence: 99%
“…Further important iron sources like heme scaffolds can be degraded in the cytosol by heme oxygenases which is accompanied by ferrous iron release, 121,122 or could be used directly as cofactors for incorporation into target proteins. 123 Iron that is released or imported in the ferric state may be subjected to a number of yet unknown reductive events before entering the main cytoplasmic trafficking routes. It can be assumed that cytosolic reduction of ferric iron also occurs in fungi, either after its cellular import via the Fet3p-Ftr1p system or after its transfer from vacuolar storage sites into the cytosol by homologous transporters like Fet5p-Fth1p in Saccharomyces.…”
Section: Intracellular Pathways For Iron Trafficking and Assimilationmentioning
confidence: 99%
“…Uroporphyrinogen decarboxylase (UroD) is a core component of heme biosynthesis (Schobert & Jahn, 2002). In addition to its electron‐carrier role in respiratory cytochromes, heme serves a variety of functions in prokaryotes, including detoxification of reactive oxygen species via its inclusion peroxidases and catalases, and regulation of various cellular processes at the level of transcription, translation, and protein stability (Dailey et al., 2017; Furuyama et al., 2007; Tiburzi et al., 2009). Previous reports have identified iron as having a key role in Wolbachia symbiosis, including heme‐mediated detoxification of reactive oxygen species by Wolbachia .…”
Section: Discussionmentioning
confidence: 99%