Journal Article

PHPPUBDB-8533

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 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. ; DESY

2008
Springer Berlin

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Please use a persistent id in citations: doi:10.1007/s00775-008-0362-y

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.

Keyword(s): Escherichia coli Proteins: chemistry (MeSH) ; Iron: chemistry (MeSH) ; Models, Molecular (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Spectrum Analysis (MeSH) ; Spectrum Analysis, Raman (MeSH) ; Sulfur: chemistry (MeSH) ; X-Rays (MeSH) ; Escherichia coli Proteins ; Recombinant Proteins ; YtfE protein, E coli ; Iron ; Sulfur

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Contributing Institute(s):

1. Experiments with synchrotron radiation (HASYLAB)
2. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. DORIS Beamline D1.2 (POF1-550) (POF1-550)

Experiment(s):

1. DORIS Beamline D1.2 (DORIS III)

Appears in the scientific report 2008

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Database coverage:
; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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