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A novel covalent modification of nitrogenase in a cyanobacterium
Author(s) -
Gallon John R.,
Cheng Jiujun,
Dougherty Lisa J.,
Gallon Victoria A.,
Hilz Helmuth,
Pederson Dennis M.,
Richards Helen M.,
Rüggeberg Sabrina,
Smith Christopher J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01229-1
Subject(s) - nitrogenase , rhodospirillum rubrum , palmitoylation , covalent bond , chemistry , biochemistry , cyanobacteria , bacteria , enzyme , nitrogen fixation , biology , cysteine , organic chemistry , genetics
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.