S. Pagani et al., PURIFICATION AND CHARACTERIZATION OF AN IRON SUPEROXIDE-DISMUTASE FROM THE NITROGEN-FIXING AZOTOBACTER-VINELANDII, FEBS letters, 357(1), 1995, pp. 79-82
Two electrophoretically distinct forms of superoxide dismutase (SOD; E
C 1.15.1.1) which show different inhibition patterns to hydrogen perox
ide have been identified in Azotobacter vinelandii. The SOD inhibited
by hydrogen peroxide was purified to homogeneity, and turned out to be
an iron superoxide dismutase, The enzyme is present in only one molec
ular form with an isoelectric point of 4.1, and it is composed of two
identical subunits with an apparent molecular weight of 21,000 Da, Spe
ctroscopic analyses indicated that this enzyme contains ferric iron (1
.4-1.6 mol/mol protein) in the typical high-spin form present in other
prokaryotic Fe-SODs, N-Terminal sequence alignments (up to the 49th r
esidue) showed that A, vinelandii Fe-SOD has high similarity with othe
r prokaryotic Fe-SODs.