Dealing with iron: Common structural principles in proteins that transport iron and heme
AUTOR(ES)
Baker, Heather M.
FONTE
National Academy of Sciences
RESUMO
Iron is essential to life, but poses severe problems because of its toxicity and the insolubility of hydrated ferric ions at neutral pH. In animals, a family of proteins called transferrins are responsible for the sequestration, transport, and distribution of free iron. Comparison of the structure and function of transferrins with a completely unrelated protein hemopexin, which carries out the same function for heme, identifies molecular features that contribute to a successful protein system for iron acquisition, transport, and release. These include a two-domain protein structure with flexible hinges that allow these domains to enclose the bound ligand and provide suitable chemistry for stable binding and an appropriate trigger for release.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=152964Documentos Relacionados
- Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction
- The Hydrogen Cold Work Peak in BCC Iron: Revisited, with First Principles Calculations and Implications for Hydrogen Embrittlement
- Vibrio cholerae iron transport systems: roles of heme and siderophore iron transport in virulence and identification of a gene associated with multiple iron transport systems.
- Absorption of hemoglobin iron: the role of a heme-splitting substance in the intestinal mucosa
- Iron transport and its relation to heme biosynthesis in Rhodopseudomonas sphaeroides.