Affinage · Plasmodium

PF3D7_1232300

cytochrome b5, putative

Annotated
2026-09-08
1 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1232300 is a putative cytochrome b5 of Plasmodium falciparum whose product localizes to the food vacuole membrane of trophozoites, where it co-localizes with a putative cytochrome b5 reductase (PF13_0353) (PMID:20493843). This co-localization has led to the proposal that the two proteins together contribute to nitric oxide generation via denitrification chemistry acting on nitrate/nitrite derived from erythrocyte cytosol (PMID:20493843). Beyond this single localization observation, no direct enzymatic activity, substrate, or mechanistic pathway has been experimentally confirmed for PF3D7_1232300 in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2010 Low

    Whether a Plasmodium cytochrome b5 has a defined subcellular home was unknown; imaging placed the PF3D7_1232300 product at the food vacuole membrane alongside a putative cytochrome b5 reductase, establishing a candidate redox module at this organelle.

    Evidence Subcellular localization by direct imaging/fractionation of food vacuoles and resonance Raman spectroscopy of intact food vacuoles in P. falciparum trophozoites

    PMID:20493843

    Open questions at the time
    • Single-lab localization experiment with no functional mutagenesis, knockout, or reconstitution to test the proposed denitrification role
    • No direct measurement of enzymatic activity or electron-transfer function for PF3D7_1232300 itself
    • Co-localization with PF13_0353 does not establish a physical complex or functional coupling

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unknown whether PF3D7_1232300 possesses any cytochrome b5 redox activity and whether it functionally participates in food-vacuole nitric oxide generation.
  • No biochemical reconstitution of PF3D7_1232300 with its putative reductase partner
  • No genetic evidence linking PF3D7_1232300 to NO/denitrification chemistry
  • No structural or heme-binding characterization of the protein

Mechanism profile

Synthesis pass · controlled-vocabulary classification

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 The product of PF3D7_1232300 (PFL1555w), a putative cytochrome b5, localizes to the food vacuole (FV) membrane of P. falciparum trophozoites, co-localizing with a putative cytochrome b5 reductase (PF13_0353); together they may contribute to NO generation via denitrification chemistry from nitrate/nitrite derived from erythrocyte cytosol. Subcellular localization by direct imaging/fractionation of food vacuoles; resonance Raman spectroscopy of intact FVs Experimental parasitology Low 20493843

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 Plasmodium falciparum: nitric oxide modulates heme speciation in isolated food vacuoles. Experimental parasitology 13 20493843