Ferrochelatase: The Convergence of the Porphyrin Biosynthesis and Iron Transport Pathways
Document Type
Article
Publication Date
2011
Keywords
ferrochelatase, iron, protoporphyrin IX, chelatase, porphyrin, tetrapyrrole, enzyme
Digital Object Identifier (DOI)
https://doi.org/10.1142/S108842461100332X
Abstract
Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. This reaction unites the biochemically synchronized pathways of porphyrin synthesis and iron transport in nearly all living organisms. The ferrochelatases are an evolutionarily diverse family of enzymes with no more than six active site residues known to be perfectly conserved. The availability of over thirty different crystal structures, including many with bound metal ions or porphyrins, has added tremendously to our understanding of ferrochelatase structure and function. It is generally believed that ferrous iron is directly channeled to ferrochelatase in vivo, but the identity of the suspected chaperone remains uncertain despite much recent progress in this area. Identification of a conserved metal ion binding site at the base of the active site cleft may be an important clue as to how ferrochelatases acquire iron, and catalyze desolvation during transport to the catalytic site to complete heme synthesis.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Porphyrins and Phthalocyanines, v. 15, issue 5, p. 350-356
Scholar Commons Citation
Hunter, Gregory A.; Al-Karadaghi, Salam; and Ferreira, Gloria C., "Ferrochelatase: The Convergence of the Porphyrin Biosynthesis and Iron Transport Pathways" (2011). Molecular Medicine Faculty Publications. 86.
https://digitalcommons.usf.edu/mme_facpub/86
