A novel covalent modification of nitrogenase in a cyanobacterium

FEBS Letters

Dougherty, Lisa J.²  Smith, Christopher J.²  Hilz, Helmuth¹  Pederson, Dennis M.²  Richards, Helen M.²  Gallon, John R.²  Gallon, Victoria A.²  Rüggeberg, Sabrina²  Cheng, Jiujun² 

[1] Institut für Physiologische Chemie, Universität Hamburg, Martinistraße 52, D-20251 Hamburg, Germany;Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, UK

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;   

DOI  :  10.1016/S0014-5793(00)01229-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown