Identification of iron superoxide dismutase and a copper/zinc superoxide dismutase enzyme activity within the marine cyanobacterium Synechococcus sp. WH 7803

Three constitutive forms of superoxide dismutase activity have been demonstrated in the cyanobacterial marine picoplankter Synechococcus sp. WH 7803 using polyacrylamide gel activity staining techniques. A protein which gave a positive non-haem iron stain on native polyacrylamide gels exhibited N-terminal similarity to both the iron superoxide dismutase and the manganese superoxide dismutase of Escherichia coli. The metal prosthetic group of each of the three activity bands was characterised by analysing their differential sensitivities to 5 mM H2O2, 2 mM cyanide and 2 mM of the copper chelator diethyldithiocarbamate. Three distinct superoxide dismutase activities were observed, an iron superoxide dismutase, a copper/zinc superoxide dismutase and a third form which has not been identified. Growth of Synechococcus cells in ASW medium containing no added iron resulted in no alteration in the activity of the iron superoxide dismutase. Growth of cultures in the absence of copper or zinc resulted in differential changes in the activities of the copper/zinc superoxide dismutase and the unidentified superoxide dismutase.