Expression and characterization of an iron-containing superoxide dismutase from Burkholderia pseudomallei

Min Hee Cho, Yong Woo Shin, Jeong Hoon Chun, Kee Jong Hong, Byoung Kuk Na, Gi eun Rhie, Baik Lin Seong, Cheon Kwon Yoo

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


A superoxide dismutase (SOD) gene from Burkholderia pseudomallei, the causative agent of melioidosis, was cloned and expressed in Escherichia coli, and its product was functionally and physically characterized. The gene has an open-reading frame of 579 bp. The deduced amino acid sequence has 192 residues with a calculated molecular mass of ~22 kDa. Sequence comparison with other bacterial SODs showed that the protein contains typical metal-binding motifs and other Fe-SOD-conserved residues. The sequence has substantial similarity with other bacterial Fe-SOD sequences. The enzymatic activity of the expressed protein was inhibited by hydrogen peroxide but not by sodium azide or potassium cyanide, attributes that indeed are characteristic of typical bacterial Fe-SODs. Western blotting with antiserum against the recombinant Fe-SOD revealed that it is expressed in B. pseudomallei. Transformed E. coli that expressed the Fe-SOD had significantly increased SOD activity and was highly tolerant to paraquat-mediated replication inhibition, compared to transformed cells carrying an empty vector. Our results provide a basis for further biochemical characterization of the enzyme and elucidation of its role in the pathogenesis of B. pseudomallei.

Original languageEnglish
Pages (from-to)1029-1033
Number of pages5
JournalJournal of Microbiology
Issue number6
Publication statusPublished - 2012 Dec

Bibliographical note

Funding Information:
This work was supported by a Korea National Institute of Health Grant (2008-N00376-00).

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology


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