Evidence for involvement of the electron transport system at a late step of anaerobic microbial heme synthesis.
The penultimate step in heme biosynthesis, the oxidation of protoporphyrinogen to protoporphyrin, can be anaerobically coupled to the reduction of fumarate in extracts of anaerobically-grown Escherichia coli. This coupling is approximately 90% inhibied by 2-heptyl-4-hydroxy quinoline-N-oxide (HQNO), a known inhibitor of the electron transport chain. This observation suggests that the mechanism of the anaerobic oxidation of protoporphyrinogen in E. coli involves a coupling into the anaerobic electron transport system. In contrast, the aerobic oxidation of protoporphyrinogen, which occurs in mammalian and yeast mitochondria, is known to be linked directly to oxygen without the mediation of an electron transport system.
D000693:Anaerobiosis; D004579:Electron Transport; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D005650:Fumarates / Q000494:pharmacology; D006418:Heme / Q000096:biosynthesis*; D006912:Hydroxyquinolines / Q000494:pharmacology; D007700:Kinetics; D011166:Porphyrins / Q000378:metabolism*; D011524:Protoporphyrins / Q000378:metabolism*
D005650:Fumarates; D006912:Hydroxyquinolines; D011166:Porphyrins; D011524:Protoporphyrins; D006418:Heme