Periplasmic Superoxide Dismutase from Desulfovibrio desulfuricans 1388 Is an Iron Protein

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M. N. Davydova^*, O. V. Gorshkov, and N. B. Tarasova

Kazan Institute of Biochemistry and Biophysics, Kazan Research Center, Russian Academy of Sciences, ul. Lobachevskogo 2/31, 420111 Kazan, Russia; fax: (8432) 292-7347; E-mail: davydova@mail.knc.ru

^* To whom correspondence should be addressed.

Received May 19, 2005; Revision received June 23, 2005

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It is shown that the genome of the sulfate-reducing bacterium Desulfovibrio desulfuricans 1388 contains a superoxide dismutase (SOD) gene (sod). The gene encodes an export signal peptide characteristic for periplasmic redox proteins. The amino acid sequence showed high homology with iron-containing SODs from other bacteria. Electrophoretically pure SOD was isolated from the periplasmic fraction of bacterial cells by FPLC chromatography. Like other Fe-SODs, D. desulfuricans 1388 superoxide dismutase is inhibited by H₂O₂ and azide, but not by cyanide.

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KEY WORDS: sulfate-reducing bacteria, Desulfovibrio desulfuricans, Fe-SOD

DOI: 10.1134/S000629790601010X

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