TY - JOUR
T1 - Mössbauer spectroscopy of Escherichia coli and its iron-storage protein
AU - Bauminger, E. R.
AU - Cohen, S. G.
AU - Dickson, D. P.E.
AU - Levy, A.
AU - Ofer, S.
AU - Yariv, J.
PY - 1980/6/26
Y1 - 1980/6/26
N2 - 57Fe Mössbauer spectra of whole frozen Escherichia coli cells and of an iron storage protein isolated from iron-rich cells of E. coli have been measured over a range of temperatures down to 0.08 K. The spectra of E. coli cells with high iron content and of the iron storage protein were found to be very similar. Above 4 K these spectra consist of a quadrupole split doublet characteristic of Fe3+. Below 3.5 K, the spectra display magnetic hyperfine splitting which is temperature dependent, and point to the existence of an ordered magnetic phase associated with a saturation magnetic hyperfine field of 43 tesla in both samples. The results indicate that the bulk of iron in the iron-rich cells is in the form of aggregates similar in nature to the iron cores in the isolated protein, although the latter account for not more than 1% of the total iron in the cells. The Mössbauer spectra of the isolated protein are different from those observed in ferritin, the iron-storage protein of plants and higher animals, showing that the iron cores in these two proteins are different.
AB - 57Fe Mössbauer spectra of whole frozen Escherichia coli cells and of an iron storage protein isolated from iron-rich cells of E. coli have been measured over a range of temperatures down to 0.08 K. The spectra of E. coli cells with high iron content and of the iron storage protein were found to be very similar. Above 4 K these spectra consist of a quadrupole split doublet characteristic of Fe3+. Below 3.5 K, the spectra display magnetic hyperfine splitting which is temperature dependent, and point to the existence of an ordered magnetic phase associated with a saturation magnetic hyperfine field of 43 tesla in both samples. The results indicate that the bulk of iron in the iron-rich cells is in the form of aggregates similar in nature to the iron cores in the isolated protein, although the latter account for not more than 1% of the total iron in the cells. The Mössbauer spectra of the isolated protein are different from those observed in ferritin, the iron-storage protein of plants and higher animals, showing that the iron cores in these two proteins are different.
KW - (Escherichia coli)
KW - Iron-storage protein
KW - Mössbauer spectroscopy
UR - http://www.scopus.com/inward/record.url?scp=0019225724&partnerID=8YFLogxK
U2 - 10.1016/0005-2795(80)90252-4
DO - 10.1016/0005-2795(80)90252-4
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C2 - 6994819
AN - SCOPUS:0019225724
SN - 0005-2795
VL - 623
SP - 237
EP - 242
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 2
ER -