TY  - JOUR
AU  - Todorovic, S.
AU  - Justino, M. C.
AU  - Wellenreuther, G.
AU  - Hildebrandt, P.
AU  - Murgida, D. H.
AU  - Meyer-Klaucke, W.
AU  - Saraiva, L. M.
AU  - DESY
TI  - Iron-sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center
JO  - Journal of biological inorganic chemistry
VL  - 13
SN  - 0949-8257
CY  - Berlin
PB  - Springer
M1  - PHPPUBDB-8533
SP  - 765-770
PY  - 2008
AB  - 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.
KW  - Escherichia coli Proteins: chemistry
KW  - Iron: chemistry
KW  - Models, Molecular
KW  - Recombinant Proteins: chemistry
KW  - Spectrum Analysis
KW  - Spectrum Analysis, Raman
KW  - Sulfur: chemistry
KW  - X-Rays
KW  - Escherichia coli Proteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - YtfE protein, E coli (NLM Chemicals)
KW  - Iron (NLM Chemicals)
KW  - Sulfur (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:18357473
UR  - <Go to ISI:>//WOS:000256320900011
DO  - DOI:10.1007/s00775-008-0362-y
UR  - https://bib-pubdb1.desy.de/record/84940
ER  -