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Iron-sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center
Citation key ISI:000256320900011
Author Todorovic, Smilja and Justino, Marta C. and Wellenreuther, Gerd and Hildebrandt, Peter and Murgida, Daniel H. and Meyer-Klaucke, Wolfram and Saraiva, Ligia M.
Pages 765-770
Year 2008
ISSN 0949-8257
DOI 10.1007/s00775-008-0362-y
Address 233 SPRING ST, NEW YORK, NY 10013 USA
Journal J. Biol. Inorg. Chem.
Volume 13
Number 5
Month JUN
Publisher SPRINGER
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 mu-oxo and mu-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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