1887

Abstract

In , NH formed by N fixation was assimilated by the glutamine synthetase-glutamate synthase pathway. The inhibition of acetylene reduction following addition of NH to N-fixing cultures was not caused by NH itself but was, most probably, related to increased intracellular levels of glutamine.

Analogues of several amino acids inhibited acetylene reduction. Apart from glutamine analogues, which interfered with NH assimilation, these analogues probably acted by inhibiting nitrogenase synthesis. Certain analogues of tryptophan and phenylalanine, which have been reported to overcome NH inhibition of cell differentiation and, possibly, nitrogenase synthesis in heterocystous cyanobacteria growing on combined nitrogen, did not prevent NH from inhibiting acetylene reduction in cultures of . In contrast, -methionine--sulphoximine, which similarly counteracts the effect of NH on heterocyst differentiation, also prevented NH from inhibiting acetylene reduction in .

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1982-04-01
2021-10-20
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