A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?
- 7 January 2000
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 287 (5450) , 122-125
- https://doi.org/10.1126/science.287.5450.122
Abstract
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).Keywords
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