In E.coli extracts under anerobic conditions catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX, transferring electrons to fumarate reductase, presumably via menaquinone. In vitro under aerobic conditions forms protoporphyrin IX using ubiquinone as an electron acceptor. Complements an E.coli hemG deletion, allowing normal growth in vivo. 3 a menaquinone + protoporphyrinogen IX = 3 a menaquinol + protoporphyrin IX 3 a ubiquinone + protoporphyrinogen IX = 3 a ubiquinol + protoporphyrin IX 3 a quinone + protoporphyrinogen IX = 3 a quinol + protoporphyrin IX Binds 1 FMN non-covalently per subunit. Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. Leishmania is not able to completely synthesize heme; it is thought that the amastigote form localized in macrophages utilizes coproporphyrinogen from the host to produce heme via the successive action of HemF, HemG and HemH. Belongs to the HemG family.