Abstract
YtfE was recently shown to be a newly discovered protein required for the recovery of the activity of iron–sulfur-containing enzymes damaged by oxidative and nitrosative stress conditions. The Escherichia coli YtfE purified protein is a dimer with two iron atoms per monomer and the type and properties of the iron center were investigated by using a combination of resonance Raman and extended X-ray absorption fine structure spectroscopies. The results demonstrate that YtfE contains a non-heme dinuclear iron center having μ-oxo and μ-carboxylate bridging ligands and six histidine residues coordinating the iron ions. This is the first example of a protein from this important class of di-iron proteins to be shown to be involved in the repair of iron–sulfur centers.
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Acknowledgments
Work in the laboratory of L.M.S. was funded by FCT project POCI/SAU-IMI/56088/2004 and a FCT SFRH/BD/13756/2003 studentship to M.C.J. We thank Miguel Teixeira for helpful discussions.
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Smilja Todorovic and Marta C. Justino contributed equally to this work.
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Todorovic, S., Justino, M.C., Wellenreuther, G. et al. Iron–sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center. J Biol Inorg Chem 13, 765–770 (2008). https://doi.org/10.1007/s00775-008-0362-y
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DOI: https://doi.org/10.1007/s00775-008-0362-y