A novel covalent modification of nitrogenase in a cyanobacterium.


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… (More)


Cite this paper

@article{Gallon2000ANC, title={A novel covalent modification of nitrogenase in a cyanobacterium.}, author={J. R. Gallon and J. Cheng and Lawrence Dougherty and Victoria A Gallon and Helmuth Hilz and Deanne Pederson and Hanno Richards and Sabrina Rueggeberg and C. J. Smith}, journal={FEBS letters}, year={2000}, volume={468 2-3}, pages={231-3} }