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. 2001 May;183(9):2970.

Rubrerythrin and Rubredoxin Oxidoreductase in Desulfovibrio vulgaris: a Novel Oxidative Stress Protection System

Heather L Lumppio 1, Neeta V Shenvi 1, Anne O Summers 1, Gerrit Voordouw 1, Donald M Kurtz Jr 1
PMCID: PMC99519

Volume 183, no. 1, p. 101–108, 2001. Page 104, Fig. 2: The deduced amino acid sequence of a putative iron or manganese-containing superoxide dismutase (Fe/Mn-SOD) from Desulfovibrio vulgaris differs from that in a more recent (but still unfinished) D. vulgaris genome sequence on The Institute for Genomic Research (TIGR) web page (updated Dec. 10, 2000). A revised Fig. 2 incorporating the TIGR-derived amino acid sequence for the D. vulgaris SOD homolog is shown below (labeled Dv). The updated residue 8 (in bold) results in a double-arginine motif characteristic of signal peptides in other bacterial redox proteins. The updated sequence reinforces our original suggestion that the mature Fe/Mn-SOD homolog in D. vulgaris would be periplasmic.

graphic file with name jb0911aux002.jpg


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