The primary structure of superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis

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Abstract
The superoxide dismutase (SOD) of Bacteroides gingivalis can use either iron or manganese as a cofactor in its catalytic activity. In this study, the complete amino acid sequence of this SOD purified from anaerobically maintained B. gingivalis cells was determined. The proteins consisted of 191 amino acid residues and had a molecular mass of 21 500. The sequence of B. gingivalis SOD showed 44–51% homology with those for iron-specific SODs (Fe-SODs) and 40–45% homology with manganese-specific SODs (Mn-SODs) from several bacteria. However, this sequence homology was considerably less than that seen among the Fe-SOD (65–74%) or Mn-SOD family (42–60%). This indicates that B. gingivalis SOD, which accepts either iron or manganese as metal cofactor, is a structural intermediate between the Fe-SOD and Mn-SOD families.