The effect of putative nucleation sites on the loading and stability of iron in ferritin

Shu Hui Juan, Steven D. Aust

研究成果: 雜誌貢獻文章同行評審

10 引文 斯高帕斯(Scopus)

摘要

The L chain of the iron storage protein ferritin contains more putative nucleation sites in the core (Glu53, 56, 57, 60, and 63) than does the H chain (Glu61, 64, and 67). Recombinant DNA techniques were used to investigate the role of these putative nucleation sites on iron loading by ceruloplasmin and on the stability of the iron core. Recombinant rat liver ferritin H chain homopolymer and the two mutants (E61A and E61A-E64A), containing three, two and one nucleation sites, respectively, loaded up to 2010 ± 50, 2010 ± 40, and 1950 ± 40 atoms of iron per ferritin, respectively. However, the mutations resulted in a 50% decrease in the rate of iron loading by ceruloplasmin. The ferritin variants incorporated the same amount of phosphate after iron loading (410 ± 20, 400 ± 30, and 420 ± 20 atoms per ferritin, respectively). The stability of the iron cores prior to phosphate incorporation, assessed by the rate of iron release by 10 mM EDTA and the paraquat cation radical, corresponded to numbers of proposed nucleation sites. The subsequent incorporation of phosphate seemed to stabilize the iron core and minimized the effect of numbers of putative nucleation sites in ferritin on the rate of iron release by EDTA and the paraquat cation radical. After incorporation of phosphate the ferritins behaved similarly to the native rat liver ferritin with respect to the rate of iron release by the paraquat cation radical.

原文英語
頁(從 - 到)259-265
頁數7
期刊Archives of Biochemistry and Biophysics
350
發行號2
DOIs
出版狀態已發佈 - 二月 15 1998
對外發佈

ASJC Scopus subject areas

  • 生物化學
  • 生物物理學
  • 分子生物學

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