Iron-sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center.

TODOROVIC, S.; JUSTINO, M. C.; WELLENREUTHER, G.; HILDEBRANDT, P.; MURGIDA, D. H.; MEYER-KLAUCKE, W.; SARAIVA, L. M.

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY

Año: 2008 vol. 13 p. 765 - 770

0949-8257

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 permonomer and the type and properties of the iron center were investigated by using a combination of resonance Raman and extended X-ray absorption fine structurespectroscopies. The results demonstrate that YtfE contains a non-heme dinuclear iron center having l-oxo and l-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 beshown to be involved in the repair of iron–sulfur centers.