Abstract
In whole cells of Rhodopseudomonas sphaeroides, nitrogen fixation, as measured by hydrogen production and acetylene reduction, was totally inhibited by micromolar concentrations of ammonia. This inhibition could not be duplicated by glutamate or glutamine alone. The inhibition by ammonia was abolished by methionine sulfoximine, a glutamine synthetase inhibitor. Inhibition by glutamine was complete in the presence of methionine sulfone, a preferential inhibitor of glutamate synthase, presumably by permitting a rise in the glutamine pool. The results indicated that the level of the glutamine pool controlled the activity of nitrogenase. None of these effects could be duplicated with cell-free nitrogenase, indicating there is probably a mediator which responds to the glutamine pool and inhibits nitrogenase, rather than glutamine itself being a direct inhibitor.
MeSH Terms
Ammonia/pharmacology
Feedback
Glutamine/metabolism,pharmacology
Kinetics
Methionine Sulfoximine/pharmacology
Nitrogenase/metabolism
Rhodobacter sphaeroides/drug effects,enzymology
Chemicals
Glutamine
Methionine Sulfoximine
Ammonia
Nitrogenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jones B L
Monty K J
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