| Type: | Family | Name: | Ferrochelatase |
| Description: | Synonym(s): Protohaem ferro-lyase, Iron chelatase, etc. Ferrochelatase catalyses the last step in haem biosynthesis: the chelation of a ferrous ion to proto-porphyrin IX, to form protohaem [, ]. In eukaryotic cells, it binds to the mitochondrial inner membrane with its active site on the matrix side of the membrane.The X-ray structure of Bacillus subtilisand human ferrochelatase have been solved [, ].The human enzyme exists as a homodimer. Each subunit contains one [2Fe-2S]cluster. The monomer is folded into two similar domains, each with a four-stranded parallelbeta-sheet flanked by an alpha-helix in a beta-alpha-beta motif that is reminiscent of the fold found in the periplasmic bindingproteins. The topological similarity between the domains suggests that they have arisen from a gene duplication event. However,significant differences exist between the two domains, including an N-terminal section (residues 80-130) that forms part of theactive site pocket, and a C-terminal extension (residues 390-423) that is involved in coordination of the [2Fe-2S]cluster and in stabilisation of the homodimer. Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals. Porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. It is likely that the structure of the cleft region will have different conformations upon substrate binding and release []. | Short Name: | Ferrochelatase |
