Iron-sulfur flavoproteins (Isf) are flavin mononucleotide (FMN)- and FeS cluster-containing proteins commonly encountered in anaerobic prokaryotes. However, with the exception of Isf from Methanosarcina thermophila, which participates in oxidative stress management by removing oxygen and hydrogen peroxide, none of these proteins has been characterized in terms of function. Trichomonas vaginalis, a sexually transmitted eukaryotic parasite of humans, was found to express several iron-sulfur flavoprotein (TvIsf) homologs in its hydrogenosomes. We show here that in addition to having oxygen-reducing activity, the recombinant TvIsf also functions as a detoxifying reductase of metronidazole and chloramphenicol, both of which are antibiotics effective against a variety of anaerobic microbes. TvIsf can utilize both NADH and reduced ferredoxin as electron donors. Given the prevalence of Isf in anaerobic prokaryotes, we propose that these proteins are central to a novel defense mechanism against xenobiotics.

• MeSH
• antitrichomonádové látky farmakologie   MeSH
• ferredoxiny metabolismus   MeSH
• flavoproteiny metabolismus   MeSH
• geny hub MeSH
• katalýza MeSH
• léková rezistence MeSH
• metronidazol chemie   farmakologie   MeSH
• molekulární sekvence - údaje MeSH
• NAD metabolismus   MeSH
• proteiny obsahující železo a síru metabolismus   MeSH
• sekvence aminokyselin MeSH
• subcelulární frakce účinky léků   metabolismus   MeSH
• Trichomonas vaginalis metabolismus   MeSH
• vodík metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH