IDENTIFICATION OF IRON SUPEROXIDE-DISMUTASE AND A COPPER ZINC SUPEROXIDE-DISMUTASE ENZYME-ACTIVITY WITHIN THE MARINE CYANOBACTERIUM SYNECHOCOCCUS SP WH-7803/
He. Chadd et al., IDENTIFICATION OF IRON SUPEROXIDE-DISMUTASE AND A COPPER ZINC SUPEROXIDE-DISMUTASE ENZYME-ACTIVITY WITHIN THE MARINE CYANOBACTERIUM SYNECHOCOCCUS SP WH-7803/, FEMS microbiology letters, 138(2-3), 1996, pp. 161-165
Three constitutive forms of superoxide dismutase activity have been de
monstrated in the cyanobacterial marine picoplankter Synechococcus sp.
WH 7803 using polyacrylamide gel activity staining techniques. A prot
ein which gave a positive non-haem iron stain on native polyacrylamide
gels exhibited N-terminal similarity to both the iron superoxide dism
utase and the manganese superoxide dismutase of Escherichia coli. The
metal prosthetic group of each of the three activity bands was charact
erised by analysing their differential sensitivities to 5 mM H2O2, 2 m
M cyanide and 2 mM of the copper chelator diethyldithiocarbamate. Thre
e distinct superoxide dismutase activities were observed, an iron supe
roxide dismutase, a copper/zinc superoxide dismutase and a third form
which has not been identified. Growth of Synechococcus cells in ASW me
dium containing no added iron resulted in no alteration in the activit
y of the iron superoxide dismutase. Growth of cultures in the absence
of copper or zinc resulted in differential changes in the activities o
f the copper/zinc superoxide dismutase and the unidentified superoxide
dismutase.