TY - JOUR
T1 - Ferritin, the path of iron into the core, as seen by Mössbauer spectroscopy
AU - Bauminger, E. R.
AU - Harrison, P. M.
N1 - Publisher Copyright:
© 2004, Kluwer Academic Publishers.
PY - 2003/12/28
Y1 - 2003/12/28
N2 - Ferritin, the ubiquitous iron storage protein, has been widely studied by a variety of techniques. The paper reviews Mössbauer studies on horse spleen and human recombinant ferritins, which helped to reveal the pathway iron follows from its uptake by the protein from a solution of Fe2SO4 to the building of the iron core of ferritin. Five different Fe(III) species and two Fe(II) species were observed, among them a peroxo-bridged and an oxo-bridged dimer, a monomer, small iron clusters and large iron aggregates. Transfer of iron between ferritin molecules was established.
AB - Ferritin, the ubiquitous iron storage protein, has been widely studied by a variety of techniques. The paper reviews Mössbauer studies on horse spleen and human recombinant ferritins, which helped to reveal the pathway iron follows from its uptake by the protein from a solution of Fe2SO4 to the building of the iron core of ferritin. Five different Fe(III) species and two Fe(II) species were observed, among them a peroxo-bridged and an oxo-bridged dimer, a monomer, small iron clusters and large iron aggregates. Transfer of iron between ferritin molecules was established.
KW - Mössbauer spectroscopy
KW - ferritin
UR - http://www.scopus.com/inward/record.url?scp=11144356119&partnerID=8YFLogxK
U2 - 10.1023/B:HYPE.0000020401.01552.56
DO - 10.1023/B:HYPE.0000020401.01552.56
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AN - SCOPUS:11144356119
SN - 0304-3843
VL - 151-152
SP - 3
EP - 19
JO - Hyperfine Interactions
JF - Hyperfine Interactions
IS - 1-4
ER -