Reconstituted and native iron-cores of bacterioferritin and ferritin.
Abstract: The structural and magnetic properties of the iron-cores of reconstituted horse spleen ferritin and Azotobacter vinelandii bacterioferritin have been investigated by high-resolution transmission electron microscopy, electron diffraction and Mossbauer spectroscopy. The structural properties of native horse spleen ferritin, native Az. vinelandii, and native and reconstituted Pseudomonas aeruginosa bacterioferritins have also been determined. Reconstitution in the absence of inorganic phosphate at pH 7.0 showed sigmoidal behaviour in each protein but was approximately 30% faster in initial rate for the Az. vinelandii protein when compared with horse spleen apoferritin. The presence of Zn2+ reduced the initial rate of Fe(II) oxidation in Az. vinelandii to 22% of the control rate. The iron-cores of the reconstituted bacterioferritins adopt defect ferrihydrite structures and are more highly ordered than their native counterparts, which are both amorphous. However, the blocking temperature for reconstituted Az. vinelandii (22.2 K) is almost identical to that for the native protein (20 K). Particle size measurements indicate that the reconstituted Az. vinelandii cores are smaller in median diameter than the native cores and this reduction in particle volume (V) offsets the increased magnetocrystalline contribution to the magnetic anisotropy constant (K) in such a way that the magnetic anisotropy barrier (KV), and hence the blocking temperature, is similar for both proteins. Reconstituted horse spleen ferritin exhibits a similar blocking temperature (38 K) to that determined for the native protein, although it is structurally more disordered. The possibility of introducing structural and compositional modifications in both horse ferritin and bacterioferritins by in-vitro reconstitution suggests that these proteins do not function primarily as a crystallochemical-specific interface for core development in vivo.
Publication Date: 1987-12-05 PubMed ID: 3123700DOI: 10.1016/0022-2836(87)90290-7Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The study investigates the structural and magnetic properties of the iron-cores of reconstituted horse spleen ferritin and Azotobacter vinelandii bacterioferritin. The findings suggest that the proteins don’t primarily function as a crystallochemical-specific interface for core development in vivo.
Investigation of Iron-cores
- The researchers used high-resolution transmission electron microscopy, electron diffraction and Mossbauer spectroscopy to investigate the structural and magnetic properties of the iron-cores of reconstituted horse spleen ferritin and Azotobacter vinelandii bacterioferritin.
- They also examined the structural properties of native horse spleen ferritin, native Az. vinelandii, and native and reconstituted Pseudomonas aeruginosa bacterioferritins.
Reconstitution and Its Effects
- Reconstitution in the absence of inorganic phosphate at pH 7.0 showed a sigmoidal behavior in each protein.
- It was noted to be approximately 30% faster in initial rate for the Az. vinelandii protein when compared with horse spleen apoferritin.
- The presence of Zn2+ reduced the initial rate of Fe(II) oxidation in Az. vinelandii to 22% of the control rate.
Structural Properties of the Iron-cores
- The iron-cores of the reconstituted bacterioferritins adopt defect ferrihydrite structures and are more highly ordered than their native counterparts, which are typically amorphous.
- The blocking temperature for reconstituted Az. vinelandii is almost identical to that for the native protein.
- The median diameter of the reconstituted Az. vinelandii cores is smaller than the native cores. This reduction in particle volume offsets the increased magnetocrystalline contribution to the magnetic anisotropy constant in such a way that the magnetic anisotropy barrier, and hence the blocking temperature, is similar for both proteins.
Implications of the Findings
- The reconstituted horse spleen ferritin shows a similar blocking temperature to that determined for the native protein, even though it is structurally more disordered.
- The potential for introducing structural and compositional modifications in both horse ferritin and bacterioferritins by in-vitro reconstitution suggests that these proteins do not primarily function as a crystallochemical-specific interface for core development in vivo.
Cite This Article
APA
Mann S, Williams JM, Treffry A, Harrison PM.
(1987).
Reconstituted and native iron-cores of bacterioferritin and ferritin.
J Mol Biol, 198(3), 405-416.
https://doi.org/10.1016/0022-2836(87)90290-7 Publication
Researcher Affiliations
- School of Chemistry, University of Bath, U.K.
MeSH Terms
- Animals
- Azotobacter / analysis
- Bacterial Proteins
- Cytochrome b Group
- Ferritins
- Horses
- Iron
- Microscopy, Electron
- Pseudomonas aeruginosa / analysis
- Spectrophotometry, Atomic
Citations
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