Effect of precipitation temperature and number of iron atoms per molecule on the structure of hydrated iron(III) oxyhydroxide ferritin cores synthesised in vitro

W. Chua-anusorn; H-R Mun; J. Webb; N.T. Gorham; T.G. St Pierre

doi:10.1023/A:1025494830924

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Effect of precipitation temperature and number of iron atoms per molecule on the structure of hydrated iron(III) oxyhydroxide ferritin cores synthesised in vitro

Journal article

Peer reviewed

Effect of precipitation temperature and number of iron atoms per molecule on the structure of hydrated iron(III) oxyhydroxide ferritin cores synthesised in vitro

W. Chua-anusorn, H-R Mun, J. Webb, N.T. Gorham and T.G. St Pierre

Hyperfine Interactions, Vol.144/145(1/4), pp.279-288

2002

DOI: https://doi.org/10.1023/A:1025494830924

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Abstract

Horse spleen apoferritin was reconstituted with varying numbers of iron atoms per protein shell at 25 and 50°C. Samples with mean particle sizes ranging from approximately 20 to 1100 iron atoms per particle were synthesised. Transmission electron microscopy combined with elemental analysis and protein assays indicated a characteristic iron density for the iron(III) oxyhydroxide of 6.4 ± 0.6 iron atoms per nm3 thus suggesting a maximum possible loading per ferritin shell of 1700 ± 200 iron atoms. Room temperature Mössbauer spectra of the iron(III) oxyhydroxide particles formed within the ferritin protein shells were doublets with slightly larger quadrupole splittings when precipitated at 25°C compared with those precipitated at 50°C. The quadrupole splittings were not significantly correlated with the number of iron atoms per protein shell although the general trend was for smaller particles to have larger quadrupole splittings. A very small but statistically significant increase in the centre shift of the Mössbauer spectra with increasing particle size was observed. These results, taken together with results from other studies, indicate that reconstituted ferritin cores are highly disordered and low density when compared with those found in native horse spleen ferritin. The results also indicate that raising the temperature of reconstitution increases the structural order within the particles slightly but that increasing the number of iron atoms per ferritin molecule above 300 has little influence on the apparent overall structural order.

Details

Title: Effect of precipitation temperature and number of iron atoms per molecule on the structure of hydrated iron(III) oxyhydroxide ferritin cores synthesised in vitro
Authors/Creators: W. Chua-anusorn (Author/Creator)
H-R Mun (Author/Creator)
J. Webb (Author/Creator)
N.T. Gorham (Author/Creator)
T.G. St Pierre (Author/Creator)
Publication Details: Hyperfine Interactions, Vol.144/145(1/4), pp.279-288
Publisher: Kluwer Academic Publishers
Identifiers: 991005542703707891
Murdoch Affiliation: School of Mathematical and Physical Sciences
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration
Citation topics: 1 Clinical & Life Sciences; 1.184 Physiology & Metals; 1.184.573 Iron Metabolism
Web Of Science research areas: Physics, Atomic, Molecular & Chemical; Physics, Condensed Matter; Physics, Nuclear
ESI research areas: Physics