FB2026_02 , released June 18, 2026
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Hernández-Gallardo, A.K., Arcos-López, T., Bahena-Lopez, J.M., Tejeda-Guzmán, C., Gallardo-Hernández, S., Webb, S.M., Kroll, T., Solari, P.L., Sánchez-López, C., Den Auwer, C., Quintanar, L., Missirlis, F. (2024). In situ detection of ferric reductase activity in the intestinal lumen of an insect.  J. Biol. Inorg. Chem. 29(7-8): 773--784.
FlyBase ID
FBrf0261215
Publication Type
Research paper
Abstract
The rise of atmospheric oxygen as a result of photosynthesis in cyanobacteria and chloroplasts has transformed most environmental iron into the ferric state. In contrast, cells within organisms maintain a reducing internal milieu and utilize predominantly ferrous iron. Ferric reductases are enzymes that transfer electrons to ferric ions, either extracellularly or within endocytic vesicles, enabling cellular ferrous iron uptake through Divalent Metal Transporter 1. In mammals, duodenal cytochrome b is a ferric reductase of the intestinal epithelium, but how insects reduce and absorb dietary iron remains unknown. Here we provide indirect evidence of extracellular ferric reductase activity in a small subset of Drosophila melanogaster intestinal epithelial cells, positioned at the neck of the midgut's anterior region. Dietary-supplemented bathophenanthroline sulphate (BPS) captures locally generated ferrous iron and precipitates into pink granules, whose chemical identity was probed combining in situ X-ray absorption near edge structure and electron paramagnetic resonance spectroscopies. An increased presence of manganese ions upon BPS feeding was also found. Control animals were fed with ferric ammonium citrate, which is accumulated into ferritin iron in distinct intestinal subregions suggesting iron trafficking between different cells inside the animal. Spectroscopic signals from the biological samples were compared to purified Drosophila and horse spleen ferritin and to chemically synthesized BPS-iron and BPS-manganese complexes. The results corroborated the presence of BPS-iron in a newly identified ferric iron reductase region of the intestine, which we propose constitutes the major site of iron absorption in this organism.
PubMed ID
PubMed Central ID
PMC11638316 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Biol. Inorg. Chem.
    Title
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
    ISBN/ISSN
    0949-8257 1432-1327
    Data From Reference
    Chemicals (2)
    Genes (2)