• Korean Journal of Microbiology
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• v.26 no.3
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• pp.215-222
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• 1988

The effect of ammonia and glutamine on nitrogenase activity of Rhodopseudomonas sphaeroides was examined. The nitrogenase activity of this strain was inhibited by ammonia and glutamine. When ammonia and glutamine were exhausted, nitrogenase activity promptly resumed at its original rate. Methionine sulfoximine (MSX), irreversible glutamine synthetase (GS) inhibitor, is a structural analogue of glutamate. MSX was used in order to know whether the nitrogenase activity was inhibited by ammonia and glutamine directly or not. The ability of MSX to prevent nitrogenase switch-off by ammonia was found to be dependent upon the phase of culture. When the cells were sampled after 12 hour culture, $500{\mu}M$ MSX would not prevent the nitrogenase switch-off by ammonia. Twenty one percents of GS actibity was inhibited by $500{\mu}M$ of MSX and concentration of released ammonia decreased. But nitrogenase activiy was still inhibited by ammonia. However, nitrogenase switch-off after 20 hours would be prevented by $100{\mu}M$ of MSX. On the other hand, GS activity was ingibited completely by $100{\mu}M$ MSX and concentration of released ammonia somewhat increased. But nitrogenase activity was not inhibited. The data indicated that the inhibition of in vivo nitrogenase actibity of Rp. sphaeroides by ammonia seemed to be mediated by products of ammonia assimilation rather than by ammonia itself.