In extracts of the unicellular cyanobacterium Gloeothece, the Fe-protein of
nitrogenase can be separated by SDS-PAGE into two antigenically identifiab
le components. Unlike the situation in photosynthetic bacteria such as Rhod
ospirillum rubrum, these two forms do not arise from covalent modification
of the protein by ADP-ribosylation. Rather, the Fe-protein of Gloeothece ni
trogenase is subjected to modification by palmitoylation, (C) 2000 Federati
on of European Biochemical Societies.