Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 13, Issue 5, Pages 765-770Publisher
SPRINGER
DOI: 10.1007/s00775-008-0362-y
Keywords
di-iron proteins; iron-sulfur repair; Raman spectroscopy; extended X-ray absorption fine structure spectroscopy
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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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