Abstract:
:Iron-sulfur cluster biosynthesis depends on protein machineries, such as the ISC and SUF systems. The reaction is proposed to imply binding of sulfur and iron atoms and assembly of the cluster within a scaffold protein followed by transfer of the cluster to recipient apoproteins. The SufA protein from Escherichia coli, used here as a model scaffold protein is competent for binding sulfur atoms provided by the SufS-SufE cysteine desulfurase system covalently as shown by mass spectrometry. Investigation of site-directed mutants and peptide mapping experiments performed on digested sulfurated SufA demonstrate that binding exclusively occurs at the three conserved cysteines (cys50, cys114, cys116). In contrast, it binds iron only weakly (K(a)=5 x 10(5)M(-1)) and not specifically to the conserved cysteines as shown by Mössbauer spectroscopy. [Fe-S] clusters, characterized by Mössbauer spectroscopy, can be assembled during reaction of sulfurated SufA with ferrous iron in the presence of a source of electrons.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sendra M,Ollagnier de Choudens S,Lascoux D,Sanakis Y,Fontecave Mdoi
10.1016/j.febslet.2007.02.058subject
Has Abstractpub_date
2007-04-03 00:00:00pages
1362-8issue
7eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00224-4journal_volume
581pub_type
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