Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

Jae Hwan Lim, Yeon Gyu Yu, In Geol Choi, Jae Ryeon Ryu, Byung-Yoon Ahn, Sung Hou Kim, Ye Sun Han

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


A superoxide dismutase (SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homooligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.

Original languageEnglish
Pages (from-to)142-146
Number of pages5
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 1997 Apr 7

Bibliographical note

Funding Information:
We thank Dr. Rosalind Kim for her advise and participation in the preparation of the manuscript. We gratefully acknowledge the support of Korea Institute of Science and Technology and a grant from Ministry of Science and Technology, Korea. The work of S.-H. Kim was supported by US Department of Energy (DOE-AC03-76S00098).


  • Aquifex
  • Hyperthermophile
  • Superoxide dismutase
  • Thermostability

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium'. Together they form a unique fingerprint.

Cite this