Jones B L, Monty K J
J Bacteriol. 1979 Sep;139(3):1007-13. doi: 10.1128/jb.139.3.1007-1013.1979.
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.
在球形红假单胞菌的全细胞中,通过氢气产生和乙炔还原测定的固氮作用,会被微摩尔浓度的氨完全抑制。单独的谷氨酸或谷氨酰胺无法产生这种抑制作用。谷氨酰胺合成酶抑制剂甲硫氨酸亚砜亚胺可消除氨的抑制作用。在谷氨酸合酶的优先抑制剂甲砜霉素存在的情况下,谷氨酰胺的抑制作用是完全的,这可能是由于谷氨酰胺池的增加所致。结果表明,谷氨酰胺池的水平控制着固氮酶的活性。这些效应在无细胞固氮酶中均无法重现,这表明可能存在一种介质,它对谷氨酰胺池做出反应并抑制固氮酶,而不是谷氨酰胺本身是直接抑制剂。