Abstract
In the photosynthetic bacterium Rhodopseudomonas capsulata, NH +4 switch-off of nitrogenase activity can be mimicked by its analog, methylamine. Like NH +4 , methylamine appeared to require processing by glutamine synthetase (GS) before it was effective; γ-glutamylmethylamide was shown to be the product of this reaction. Evidence that this glutamine analog functioned directly to initiate nitrogenase inactivation was suggested first by the fact that it was a poor substrate for glutamate synthase (i.e., it was not further metabolized by this pathway) and secondly, azaserine which blocks the transfer of the glutamine amide group had no effect on CH3NH +3 (or NH +4 ) switch-off. These observations are taken as preliminary evidence to suggest that when NH +4 inhibits nitrogenase activity, inactivation is initiated by glutamine itself, and not a molecule derived from it. Finally, evidence was presented that R. capsulata would use CH3NH +3 as a nitrogen substrate, but lag periods and generation times increased with subsequent passages.
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Yoch, D.C., Zhang, Zm. & Claybrook, D.L. Methylamine metabolism and its role in nitrogenase “Switch off” in Rhodopseudomonas capsulata . Arch. Microbiol. 134, 45–48 (1983). https://doi.org/10.1007/BF00429405
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DOI: https://doi.org/10.1007/BF00429405