R. George Ratcliffe

Abstract Nitrate and ammonium have different effects on many biochemical and physiological processes in plants, and at high concentrations this can lead to markedly different growth responses. Most plant species show reduced growth, smaller leaves and a stunted root system when exposed to high ammonium concentrations, and in severe cases this leads to chlorosis. Although well known, ammonium toxicity is poorly understood and is generally considered to be the result of one or more of the following effects; (i) ammonium‐induced mineral nutrient deficiency, arising from the impaired uptake of metal ions; (ii) secondary growth inhibition arising from the acidification of the rooting medium; (iii) alterations in intracellular pH and osmotic balance; (iv) uncoupling of photophosphorylation from electron transport, following the accumulation of ammonium in leaves; and (v) altered polyamine and phytohormone metabolism. These hypotheses are reviewed in the light of the available literature and experimental evidence from own experiments. It is concluded that no mechanism on its own provides an adequate explanation of the available data.

Transgenic tomato (Solanum lycopersicum) plants expressing a fragment of the mitochondrial malate dehydrogenase gene in the antisense orientation and exhibiting reduced activity of this isoform of malate dehydrogenase show enhanced photosynthetic activity and aerial growth under atmospheric conditions (360 ppm CO2). In comparison to wild-type plants, carbon dioxide assimilation rates and total plant dry matter were up to 11% and 19% enhanced in the transgenics, when assessed on a whole-plant basis. Accumulation of carbohydrates and redox-related compounds such as ascorbate was also markedly elevated in the transgenics. Also increased in the transgenic plants was the capacity to use L-galactono-lactone, the terminal precursor of ascorbate biosynthesis, as a respiratory substrate. Experiments in which ascorbate was fed to isolated leaf discs also resulted in increased rates of photosynthesis providing strong indication for an ascorbate-mediated link between the energy-generating processes of respiration and photosynthesis. This report thus shows that the repression of this mitochondrially localized enzyme improves both carbon assimilation and aerial growth in a crop species.

Abstract Transgenic tomato ( Solanum lycopersicum ) plants expressing a fragment of a fumarate hydratase (fumarase) gene in the antisense orientation and exhibiting considerable reductions in the mitochondrial activity of this enzyme show impaired photosynthesis. The rate of the tricarboxylic acid cycle was reduced in the transformants relative to the other major pathways of carbohydrate oxidation and the plants were characterized by a restricted rate of dark respiration. However, biochemical analyses revealed relatively little alteration in leaf metabolism as a consequence of reducing the fumarase activity. That said, in comparison to wild‐type plants, CO 2 assimilation was reduced by up to 50% under atmospheric conditions and plants were characterized by a reduced biomass on a whole plant basis. Analysis of further photosynthetic parameters revealed that there was little difference in pigment content in the transformants but that the rate of transpiration and stomatal conductance was markedly reduced. Analysis of the response of the rate of photosynthesis to variation in the concentration of CO 2 confirmed that this restriction was due to a deficiency in stomatal function.

In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated (15)N/(13)C mass spectrometry have been used to demonstrate that glutamate dehydrogenase is active in the oxidation of glutamate, but not in the reductive amination of 2-oxogiutarate. In cell suspension cultures of carrot (Daucus carota L. cv Chantenay), primary assimilation of ammonium occurs via the glutamate synthase pathway. Glutamate dehydrogenase is derepressed in carbonlimited cells and in such cells the function of glutamate dehydrogenase appears to be the oxidation of glutamate, thus ensuring sufficient carbon skeletons for effective functioning of the tricarboxylic acid cycle. This catabolic role for glutamate dehydrogenase implies an important regulatory function in carbon and nitrogen metabolism.