| Literature DB >> 10692592 |
J R Gallon1, J Cheng, L J Dougherty, V A Gallon, H Hilz, D M Pederson, H M Richards, S Rüggeberg, C J Smith.
Abstract
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.Entities:
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Year: 2000 PMID： 10692592 DOI： 10.1016/s0014-5793(00)01229-1
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124