Mutational analysis of loading of iron into rat liver ferritin by ceruloplasmin

Shu H. Juan, Steven D. Aust

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Site-directed mutagenesis was used to investigate the loading of iron into rat liver ferritin by ceruloplasmin. Changes were made in the H chain to investigate the role of tyrosines involved in an inherent ferroxidase activity thought to be involved in the self-loading of iron into ferritin. Mutation Y34F affected the rate of iron loading by ceruloplasmin and incorporation of the oxidized iron into the core. Mutation Y29R (making it analogous to the L chain) had no effect on iron oxidation but slightly decreased core formation. A double mutation in the L chain, to open the α- helix bundle channel, and R25Y, making the protein more analogous to the H chain, increased the amount of iron incorporated into the core, again suggesting that this Tyr is involved in ligand exchange for core formation. Additional changes in the L chain involving the BC loop suggest that the entire BC loop is involved in the association of ferritin with ceruloplasmin, increasing its ferroxidase activity and the rate of iron loading into ferritin.

Original languageEnglish
Pages (from-to)295-301
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume361
Issue number2
DOIs
Publication statusPublished - Jan 15 1999
Externally publishedYes

Fingerprint

Ceruloplasmin
Ferritins
Liver
Rats
Iron
Mutation
Mutagenesis
Site-Directed Mutagenesis
Tyrosine
Association reactions
Ligands
Oxidation

Keywords

  • Ceruloplasmin
  • Ferritin
  • Iron

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Mutational analysis of loading of iron into rat liver ferritin by ceruloplasmin. / Juan, Shu H.; Aust, Steven D.

In: Archives of Biochemistry and Biophysics, Vol. 361, No. 2, 15.01.1999, p. 295-301.

Research output: Contribution to journalArticle

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