Abstract
Upon addition of ammonium or removal of light, nitrogenase was reversibly inactivated in a draTG gene deletion mutant of Rhodobacter capsulatus. Reversible inactivation by exposure of the mutant to darkness followed the same kinetics as in control strains containing the draTG gene region. Reactivation of nitrogenase by light was significantly faster than removal of ADP-ribose from component 2 of nitrogenase. The results show that, in R. capsulatus, reversible inactivation of nitrogenase is independent of reversible ADP-ribosylation by the DRAT/DRAG enzyme system encoded by the draTG gene region.
Full Text
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call