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Science 7 January 2000:
Vol. 287. no. 5450, pp. 122 - 125
DOI: 10.1126/science.287.5450.122
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Reports

A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?

Jungwon Hwang, 1 Carsten Krebs, 2 Boi Hanh Huynh, 2 Dale E. Edmondson, 3 Elizabeth C. Theil, 4 James E. Penner-Hahn 1*

The reaction of oxygen with protein diiron sites is important in bioorganic syntheses and biomineralization. An unusually short Fe-Fe distance of 2.53 angstroms was found in the diiron (µ-1,2 peroxodiferric) intermediate that forms in the early steps of ferritin biomineralization. This distance suggests the presence of a unique triply bridged structure. The Fe-Fe distances in the µ-1,2 peroxodiferric complexes that were characterized previously are much longer (3.1 to 4.0 angstroms). The 2.53 angstrom Fe-Fe distance requires a small Fe-O-O angle (~106° to 107°). This geometry should favor decay of the peroxodiferric complex by the release of H2O2 and µ-oxo or µ-hydroxo diferric biomineral precursors rather than by oxidation of the organic substrate. Geometrical differences may thus explain how diiron sites can function either as a substrate (in ferritin biomineralization) or as a cofactor (in O2 activation).

1 Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
2 Department of Physics,
3 Departments of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA.
4 Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609-1673, USA.
*   To whom correspondence should be addressed. E-mail: jeph{at}umich.edu

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