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FEBS Lett. 2000 Feb 25;468(2-3):231-3.

A novel covalent modification of nitrogenase in a cyanobacterium.

Author information

1
Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, UK. j.r.gallon@swansea.ac.uk

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.

PMID:
10692592
DOI:
10.1016/s0014-5793(00)01229-1
[Indexed for MEDLINE]
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