Blue-green algae (cyanobacteria) have evolved as the most primitive, oxygen
ic, plant-type photosynthetic organisms. Within a single prokaryotic cell,
they have uniquely accommodated both oxygenic photosynthesis and aerobic re
spiration, which are known to produce superoxide and hydrogen peroxide as i
nevitable byproducts. Two types of superoxide dismutase have been character
ized in both N-2-fixing and non-N-2-fixing cyanobacteria, namely cytosolic
iron-containing superoxide dismutase and thylakoid-bound manganese-containi
ng superoxide dismutase. No qualitative differences between various cell ty
pes (vegetative cells, heterocysts) were found. In contrast to chloroplasts
, most of the cyanobacterial species show catalatic activity. From two spec
ies the corresponding enzymes have been characterized as typical prokaryoti
c (bifunctional) catalase-peroxidases with homologies to cytochrome c perox
idases and ascorbate peroxidases. In addition to catalatic activity, some s
trains exhibit ascorbate peroxidase activity, but to dale there are no repo
rts detailing purification and characterization.
Cyanobacteria were found to contain low intracellular ascorbate concentrati
ons (30-100 mu M) and 2-5 mM glutathione. Both monodehydroascorbate and glu
tathione reductase activities were detected in most species examined, where
as dehydroascorbate reductase activity was absent. The question as to wheth
er a glutathione-ascorbate cycle exists in cyanobacteria cannot be answered
at present.