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J Biol Chem, Vol. 274, Issue 45, 32402-32410, November 5, 1999
From the During the purification of site-directed mutant
variants of Azotobacter vinelandii ferredoxin I (FdI), a
pink protein, which was not observed in native FdI preparations,
appeared to associate specifically with variants that had mutations in
ligands to FdI [Fe-S] clusters. That protein, which we designate
FdIV, has now been purified. NH2-terminal sequence analysis
revealed that the protein is the product of a previously described
gene, herein designated fdxD, that is in the A. vinelandii iscSUA operon that encodes proteins involved in
iron-sulfur cluster assembly or repair. An apoprotein molecular mass of
12,434.03 ± 0.21 Da was determined by mass spectrometry
consistent with the known gene sequence. The monomeric protein was
shown to contain a single [2Fe-2S]2+/+ cluster by
UV/visible, CD, and EPR spectroscopies with a reduction potential of
Purification and Biophysical Characterization of a New [2Fe-2S]
Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S]
Cluster Assembly/Repair Protein
,,
Department of Molecular Biology and
Biochemistry, University of California, Irvine, California 92697 and the ¶ Department of Biochemistry, Virginia Polytechnic
Institute and State University, Blacksburg, Virginia 24061
344 mV versus the standard hydrogen electrode. When overexpressed in Escherichia coli, recombinant FdIV
holoprotein was successfully assembled. However, the polypeptide of the
recombinant protein was modified in some way such that the apoprotein
molecular mass increased by 52 Da. Antibodies raised against FdIV and
EPR spectroscopy were used to examine the relative levels of FdIV and
FdI in various A. vinelandii strains leading to the
conclusion that FdIV levels appear to be specifically increased under
conditions where another protein, NADPH:ferredoxin reductase is also
up-regulated. In that case, the fpr gene is known to be
activated in response to oxidative stress. This suggests that the
fdxD gene and other genes in the iron-sulfur cluster
assembly or repair operon might be similarly up-regulated in response
to oxidative stress.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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