How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli

FEBS Lett. 1998 Aug 7;432(3):213-8. doi: 10.1016/s0014-5793(98)00867-9.

Abstract

The iron storage proteins, ferritins, are found in all organisms which use iron. Here iron storage processes in the Escherichia coli ferritin (EcFtnA) are compared with those in human H-type ferritin (HuHF). Both proteins contain dinuclear iron centres that enable the rapid oxidation of 2 Fe(II) by O2. The presence of a third iron binding site in EcFtnA, although not essential for fast oxidation, causes the O2/Fe ratio to increase from 2 to 3-4. In EcFtnA the rate of iron oxidation falls markedly after the oxidation of 48 Fe(II) atoms/molecule probably because some of it remains at the oxidation site. However a compensatory physiological advantage is conferred because this iron is more readily available to meet the cell's needs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism*
  • Ferritins / chemistry
  • Ferritins / metabolism*
  • Ferrous Compounds / chemistry
  • Ferrous Compounds / metabolism
  • Iron / metabolism*
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Oxygen / metabolism
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Ferrous Compounds
  • Ferritins
  • Iron
  • Oxygen