Iron-sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center.
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.
Todorovic
Smilja
S
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal.
Justino
Marta C
MC
Wellenreuther
Gerd
G
Hildebrandt
Peter
P
Murgida
Daniel H
DH
Meyer-Klaucke
Wolfram
W
Saraiva
Lígia M
LM
D029968:Escherichia coli Proteins / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D011994:Recombinant Proteins / Q000737:chemistry; D013057:Spectrum Analysis; D013059:Spectrum Analysis, Raman; D013455:Sulfur / Q000737:chemistry*; D014965:X-Rays
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; C497162:YtfE protein, E coli; D013455:Sulfur; D007501:Iron