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Nitrogenase activity in the photosynthetic bacterium Rhodospirillum rubrum is reversibly regulated by interconversion of the Fe protein between a modified and an unmodified form. Since the discovery of the activation process in 1976, investigators have been unable to demonstrate the inactivation (modification) reaction in vitro. In this study, NAD-dependent modification and concomitant inactivation of the Fe protein were demonstrated in crude extracts of R. rubrum. Activation of the in vitro-modified Fe protein by activating enzyme and structural similarity between the in vivo and in vitro modifications are presented as evidence that the in vitro modification is the physiologically relevant ADP-ribosylation reaction. Using a partially purified preparation, we showed that the inactivating enzyme activity is stimulated by divalent metal ions and ADP, that O2-denatured Fe protein will not serve as a substrate, and that dithionite inhibits the modification reaction.
R G Lowery, and
L L Saari, and
P W Ludden
November 1991,
Journal of bacteriology,
R G Lowery, and
L L Saari, and
P W Ludden
January 1989,
Current topics in cellular regulation,
R G Lowery, and
L L Saari, and
P W Ludden
January 2015,
Current topics in microbiology and immunology,
R G Lowery, and
L L Saari, and
P W Ludden
October 1976,
Science (New York, N.Y.),
R G Lowery, and
L L Saari, and
P W Ludden
July 2000,
Journal of bacteriology,
R G Lowery, and
L L Saari, and
P W Ludden
September 1989,
Journal of bacteriology,
R G Lowery, and
L L Saari, and
P W Ludden
April 1986,
The Journal of biological chemistry,
R G Lowery, and
L L Saari, and
P W Ludden
December 1982,
The Journal of biological chemistry,
R G Lowery, and
L L Saari, and
P W Ludden
September 1982,
The Biochemical journal,
R G Lowery, and
L L Saari, and
P W Ludden
March 1983,
The Biochemical journal,
