A novel covalent modification of nitrogenase in a cyanobacterium

[摘要]

In extracts of the unicellular cyanobacterium Gloeothece, the Fe-protein of nitrogenase can be separated by SDS–PAGE into two antigenically identifiable components. Unlike the situation in photosynthetic bacteria such as Rhodospirillum rubrum, these two forms do not arise from covalent modification of the protein by ADP-ribosylation. Rather, the Fe-protein of Gloeothece nitrogenase is subjected to modification by palmitoylation.

[学科分类] 生物化学/生物物理

[关键词] Covalent modification;Cyanobacterium;Fe-protein;Nitrogenase;Palmitoylation;Gloeothece;HEPES;N-2-hydroxyethylpiperazine-N′-2-ethanesulphonic acid;HPTLC;high performance thin layer chromatography;MALDI;matrix-assisted laser desorption;PAGE;polyacrylamide gel electrophoresis;PPO;2;5-diphenyloxazole;TOF;time of flight