Modulation in isocitrate dehydrogenase activity under citrate enrichment affects carbon and nitrogen fixations in the cyanobacterium Nostoc muscorum Meg 1

The enzyme isocitrate dehydrogenase (IDH) converts isocitrate synthesized from citrate to α-ketoglutarate in the TCA cycle. In cyanobacteria, α-KG has an additional role where it donates its carbon skeleton for ammonium assimilation in the GS-GOGAT pathway thereby linking carbon and nitrogen metabolisms. Looking at this crucial function of IDH that makes α-KG available for both carbon and nitrogen assimilation, changes brought about in its activity under excess availability of citrate in a cyanobacterium was evaluated. Further, how these changes are transmitted downstream affecting carbon and nitrogen metabolisms were also evaluated. A 100 μM citrate supplementation induced IDH activity. Consequently, there was an increase in concentrations of photosynthetic pigments, D1 protein and RuBisCO as well as in PSII activity. Heterocyst differentiation was initiated and an upsurge in the activities of nitrogenase and GS were recorded. An enhancement in the total protein and carbohydrate content reiterated the positive influence of citrate enrichment on carbon and nitrogen fixation. The increase in the mRNA contents of IDH, D1 protein, RuBisCO, nitrogenase and GS indicated their induction at the genetic level. Finally, there was augmentation in total biomass production by ∼28%. Interestingly as citrate concentration was increased to 500 μM, both C- and N- fixations were highly compromised suggesting that even though citrate is an essential metabolite in the cells, it became toxic beyond a certain concentration to the organism. SEM and TEM studies showed no changes in the organism's morphology and ultra-structure in presence of 100 μM citrate while adverse changes were noticed in presence of 500 μM citrate.