Trichomonas vaginalis ハイドロゲノソームのプロテオームはミトコンドリアと比較して大幅に縮小しているが、マイトソームよりも複雑である
Trichomonas vaginalis, a human pathogen, lacks conventional mitochondria and instead harbors hydrogenosomes — double-membrane organelles that generate molecular hydrogen. A detailed proteomic survey of purified hydrogenosomes identified 569 proteins, a figure markedly lower than the 1,000–1,500 proteins documented in fungal and animal mitochondrial proteomes but substantially greater than those assigned to mitosomes. Functional categories accounting for roughly 30% of the proteome include amino acid and energy metabolism, Fe-S cluster assembly, flavin-mediated catalysis, oxygen stress response, membrane translocation, chaperonin activity, proteolytic processing, and ATP hydrolysis. GTPases and ribosomal proteins appear concentrated on the organelle's outer surface, and glycolytic proteins were also detected, mirroring observations in mitochondrial proteomes. Approximately 18% of identified proteins are hypothetical with unknown functions, suggesting that many hydrogenosomal activities remain to be characterized.
Hydrogenosomes share a common evolutionary origin with mitochondria and produce molecular hydrogen through anaerobic energy metabolism involving Fe-S cluster assembly and flavin-mediated catalysis, supporting ATP generation in the absence of oxygen.
This is basic research at the cellular or molecular level. For human application, inhalation is the most promising delivery route, but inhalation carries explosion risk and concentration matters (empirical LFL of 10%; high-concentration devices are not recommended).
See also:
https://h2-papers.org/en/papers/22079833