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Science 5 February 1993:
Vol. 259. no. 5096, pp. 796 - 798
DOI: 10.1126/science.8430332
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Articles

Science, Vol 259, Issue 5096, 796-798
Copyright © 1993 by American Association for the Advancement of Science

articles

Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin

GS Waldo, J Ling, J Sanders-Loehr, and EC Theil

Department of Biochemistry, North Carolina State University, Raleigh 27695.

An iron(III)-tyrosinate complex was identified in ferritin by ultraviolet-visible and resonance Raman spectroscopies. Previously, a specific amino acid side chain coordinated to iron in ferritin was not known. Ferritin protein was overexpressed in Escherichia coli from complementary DNA sequences of bullfrog red cell ferritin. The purple iron(III)-tyrosinate intermediate that formed during the first stages of iron uptake was replaced by the amber multinuclear iron(III)-oxo complexes of fully mineralized ferritin. Only the H subunit formed detectable amounts of the iron(III)-tyrosinate complex, which may explain the faster rates of iron biomineralization in H- compared to L-type ferritin.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Iron uptake in ferritin is blocked by binding of [Cr(TREN)(H2O)(OH)]2+, a slow dissociating model for [Fe(H2O)6]2+.
C. M. Barnes, E. C. Theil, and K. N. Raymond (2002)
PNAS 99, 5195-5200
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Localized Unfolding at the Junction of Three Ferritin Subunits. A MECHANISM FOR IRON RELEASE?.
H. Takagi, D. Shi, Y. Ha, N. M. Allewell, and E. C. Theil (1998)
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Role of H and L Subunits in Mouse Ferritin.
P. Rucker, F. M. Torti, and S. V. Torti (1996)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)