Initial characterization of an iron superoxide dismutase from Thermobifida fusca.

ABSTRACT: Superoxide dismutases (SODs) are enzymes that catalyze the dismutation of the superoxide radical anion into O₂ and H₂O₂ in a two-step reaction. They are ubiquitous to all forms of life and four different types of metal centers are detected, dividing this class of enzymes into Cu-/Zn-, Ni-, Mn-, and Fe-SODs. In this study, a superoxide dismutase from the thermophilic bacteria Thermobifida fusca (TfSOD) was cloned and expressed before the recombinant enzyme was characterized. The enzyme was found to be active for superoxide dismutation measured by inhibition of cytochrome c oxidation and the inhibition of the autoxidation of pyrogallol. Its pH-optimum was determined to be 7.5, while it has a broad temperature optimum ranging from 20 to 90 °C. Combined with th

SUBMITTER: Hamre AG 

PROVIDER: S-EPMC10520107 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature