Ferrochelatase

Function Ferrochelatase (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Sirohydrochlorin ferrochelatase (SirB) catalyzes the addition of Fe+2 to sirohydrochlorin to produce siroheme. Disease Defective FECH is the cause of erythropoietic protoporphyria (EPP), an inherited disorder of heme synthesis . Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase Ferrochelatase produces . It can also . However, the ability to insert other . In this way Bacillus subtilis ferrochelatase can insert copper into protoporphyrin IX, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. shows that , while A third residue, Tyr in B. subtilis, is a third ligand via a water molecule. Human and S. cerevisiae ferrochelatase utilizes In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the is a . By site directed mutagenesis and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase . Two crystal structures are presented. how . The how a in the B. subtilis enzyme. 3D structures of ferrochelatase Ferrochelatase 3D structures

spinqualitylabelsall models Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code 1c1h) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image