Biomineralization of iron: Moessbauer spectroscopy and electron microscopy of ferritin cores from the chiton Acanthopleura hirtosa and the limpet Patella laticostata

T.G. St Pierre; K.S. Kim; J. Webb; S. Mann; D.P.E. Dickson

doi:10.1021/ic00335a022

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Biomineralization of iron: Moessbauer spectroscopy and electron microscopy of ferritin cores from the chiton Acanthopleura hirtosa and the limpet Patella laticostata

Journal article

Peer reviewed

Biomineralization of iron: Moessbauer spectroscopy and electron microscopy of ferritin cores from the chiton Acanthopleura hirtosa and the limpet Patella laticostata

T.G. St Pierre, K.S. Kim, J. Webb, S. Mann and D.P.E. Dickson

Inorganic Chemistry, Vol.29(10), pp.1870-1874

1990

DOI: https://doi.org/10.1021/ic00335a022

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Abstract

Ferritins isolated from the hemolymph of the chiton Acanthopleura hirtosa and the limpet Patella laticostata have been studied by 57Fe Mössbauer spectroscopy, electron diffraction, transmission electron microscopy (TEM), and inductively coupled plasma (ICP) spectrometry. Mössbauer spectra of the samples at 78 K were quadrupole-split doublets with similar quadrupole splittings and chemical isomer shifts, characteristic of octahedral high-spin iron(III), while at 4.2 K the spectra were magnetically split sextets. The spectra yield mean superparamagnetic blocking temperatures of about 32 and 30 K for the A. hirtosa and P. laticostata ferritins, respectively, and indicate magnetic ordering temperatures of about 37 and 34 K. Core size distributions were measured for both the A. hirtosa and P. laticostata ferritins by using TEM and gave mean core size ranges of 8.0-8.5 and 7.5-8.0 nm, respectively. Diffuse lines in the electron diffraction patterns of the ferritin cores indicated the presence of ferrihydrite (5Fe2-O3·9H2O) of limited crystallinity. Phosphorus to iron atomic ratios were measured by ICP spectrometry. The phosphorus levels were close to the limit of detection, giving approximate mean values of P:Fe of 1:44 for the P. laticostata ferritin and 1:36 for the A. hirtosa ferritin. These levels of phosphate are significantly less than those for the crystalline cores of mammalian ferritins and considerably less than those for the noncrystalline core of bacterioferritins.

Details

Title: Biomineralization of iron: Moessbauer spectroscopy and electron microscopy of ferritin cores from the chiton Acanthopleura hirtosa and the limpet Patella laticostata
Authors/Creators: T.G. St Pierre (Author/Creator)
K.S. Kim (Author/Creator)
J. Webb (Author/Creator)
S. Mann (Author/Creator)
D.P.E. Dickson (Author/Creator)
Publication Details: Inorganic Chemistry, Vol.29(10), pp.1870-1874
Publisher: American Chemical Society
Identifiers: 991005540680607891
Copyright: © 1990 American Chemical Society.
Murdoch Affiliation: School of Mathematical and Physical Sciences
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Citation topics: 1 Clinical & Life Sciences; 1.184 Physiology & Metals; 1.184.573 Iron Metabolism
Web Of Science research areas: Chemistry, Inorganic & Nuclear
ESI research areas: Chemistry