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Structural basis for iron mineralization by bacterioferritin.

Allister Crow1, Tamara L Lawson, Allison Lewin

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This study reveals how bacterioferritin (BFR) mineralizes iron, showing its ferroxidase center acts as a catalytic cofactor. A novel inner iron site aids electron transfer, suggesting BFR

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Ferritin proteins manage cellular iron through mineralization within their core.
  • Bacterioferritin (BFR) is a bacterial ferritin with a distinct iron mineralization mechanism.
  • Understanding BFR's mechanism provides insights into iron homeostasis and evolution.

Purpose of the Study:

  • To elucidate the mechanism of iron mineralization in bacterioferritin (BFR).
  • To characterize the role of the ferroxidase center and novel iron-binding sites in BFR.
  • To compare BFR's mechanism with eukaryotic ferritins and related proteins.

Main Methods:

  • X-ray crystallography to determine BFR structures (apo, di-Fe(2+), di-Fe(3+)).
  • Kinetic studies of wild-type and mutant BFR variants.
  • Analysis of iron binding sites and electron transfer pathways.

Main Results:

  • The BFR ferroxidase center is preformed for Fe(2+) binding and oxidation.
  • A stable mu-oxo bridged di-Fe(3+) center is formed, with no direct transfer to the core.
  • A novel inner surface Fe(2+) site (His46, Asp50) is identified and functionally validated.
  • The ferroxidase center acts catalytically, distinct from eukaryotic ferritin pore models.
  • The inner surface site facilitates electron transfer for Fe(2+) oxidation.

Conclusions:

  • Bacterioferritin utilizes a catalytic ferroxidase center for iron mineralization.
  • A novel inner iron site is crucial for electron transfer in BFR.
  • BFR's mechanism may represent an evolutionary link to other di-iron proteins.