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J. Biol. Chem., Vol. 275, Issue 21, 15669-15675, May 26, 2000
From the Class III anaerobic ribonucleotide reductase
small component, named protein
The Activating Component of the Anaerobic Ribonucleotide
Reductase from Escherichia coli
AN IRON-SULFUR CENTER WITH ONLY THREE CYSTEINES*
§¶,§,
,,, and**
Laboratoire de Chimie et Biochimie des
Centres Rédox Biologiques, Commissariat à l'Energie
Atomique/Département de Biologie Moléculaire et
Structurale, EP 1087 CNRS, Université Joseph Fourier, 17, rue des
Martyrs, 38054 Grenoble Cédex 9, France and the Institut
für Physik, Medizinische Universität,
D-23538 Lübeck, Germany
, contains a (4Fe-4S) center. Its
function is to mediate electron transfer from reduced flavodoxin to
S-adenosylmethionine, required for the introduction of a
glycyl radical in the large component, named protein 
, which then
becomes active for the reduction of ribonucleotides. By site-directed
mutagenesis we demonstrate that the three cysteines of the conserved
CXXXCXXC sequence are involved in iron
chelation. Such a sequence is also present in the activase of the
pyruvate formate-lyase and in the biotin synthase, both carrying an
iron-sulfur center involved in reductive activation of
S-adenosylmethionine. Even though they are able to bind
iron in the (4Fe-4S) form, as shown by Mössbauer spectroscopy,
the corresponding Cys to Ala mutants are catalytically inactive.
Mutation of the two other cysteines of the protein did not result in
inactivation. We thus conclude that the (4Fe-4S) cluster has, in the
wild type protein, only three cysteine ligands and a fourth still
unidentified ligand.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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