Examination of the Nickel Site Structure in Streptomyces seoulensis Superoxide Dismutase by EPR and X-ray Absorption Spectroscopy

  • Lee, Jin-Won (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
  • Yim, Yang-In (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
  • Michael J. Maroney (Department of Chemistry and the Program in Molecular and Cellular Biology, University of Massachusett) ;
  • Kang, Sa-Ouk (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University)
  • Published : 1998.06.01

Abstract

Superoxide dismutases are metalloenzymes catalyzing the dimutation of superoxide anion radical to hydrogen peroxide and molecular oxygen. Examples of enzymes containing Cu, Mn and Fe as the redox-active metal have been characterized. Recently, an SOD containing one Ni atom per subunit was reported.(omitted)

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