WebProbably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. WebHere, we report that a radical SAM protein, the heme chaperone HemW from bacteria, is required for the insertion of heme b into respiratory chain …

The radical SAM protein HemW is a heme chaperone

WebOct 1, 2024 · The fate of heme in gram-positive bacteria after its final biosynthesis was not known until the identification of HemW which showed that this heme-recipient protein is a … WebJul 10, 2014 · The radical SAM superfamily (RSS) contains a tremendous number of homologous enzymes that catalyze a remarkably broad range of reactions (Lanz & Booker, 2015; Wang et al., 2014). They exhibit... spiral or comma shaped bacteria

Recent Advances in Radical SAM Enzymology: New Structures …

WebFeb 16, 2024 · Here, we report that a radical SAM protein, the heme chaperone HemW from bacteria, is required for the insertion of heme b into respiratory chain enzymes. As other … WebHemN is a radical S -adenosylmethionine (SAM) enzyme that catalyzes the anaerobic oxidative decarboxylation of coproporphyrinogen III to produce protoporphyrinogen IX, a key intermediate in heme biosynthesis. Proteins homologous to HemN (HemN-like proteins) are widespread in both prokaryotes and eukaryotes. WebAs other radical SAM proteins, HemW contains three cysteines and one SAM coordinating an [4Fe-4S] cluster, and we observed one heme per subunit of HemW. We found that an … spiral orchid residence in bahrain