Advanced

Ferrochelatase: the convergence of the porphyrin biosynthesis and iron transport pathways

Hunter, Gregory A.; Al-Karadaghi, Salam LU and Ferreira, Gloria C. (2011) In Journal of Porphyrins and Phthalocyanines 15(5-6). p.350-356
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
ferrochelatase, iron, protoporphyrin IX, chelatase, porphyrin, tetrapyrrole, enzyme
in
Journal of Porphyrins and Phthalocyanines
volume
15
issue
5-6
pages
350 - 356
publisher
Society of Porphyrins & Phthalocyanines
external identifiers
  • wos:000292646900005
  • scopus:79960341461
ISSN
1099-1409
DOI
10.1142/S108842461100332X
language
English
LU publication?
yes
id
3a3116df-1893-4e2f-a68c-9f1fdca8a66d (old id 2094022)
date added to LUP
2011-08-25 12:00:39
date last changed
2017-04-23 03:18:28
@article{3a3116df-1893-4e2f-a68c-9f1fdca8a66d,
  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.},
  author       = {Hunter, Gregory A. and Al-Karadaghi, Salam and Ferreira, Gloria C.},
  issn         = {1099-1409},
  keyword      = {ferrochelatase,iron,protoporphyrin IX,chelatase,porphyrin,tetrapyrrole,enzyme},
  language     = {eng},
  number       = {5-6},
  pages        = {350--356},
  publisher    = {Society of Porphyrins & Phthalocyanines},
  series       = {Journal of Porphyrins and Phthalocyanines},
  title        = {Ferrochelatase: the convergence of the porphyrin biosynthesis and iron transport pathways},
  url          = {http://dx.doi.org/10.1142/S108842461100332X},
  volume       = {15},
  year         = {2011},
}