Reduction of nitrogenous oxides by microorganisms.

Treatments of inorganic nutrition tend to become listings of poorly related facts and observations. As more information becomes available, this should give way to a drawing together of observations in an attempt to find new insights into the metabolic roles of nutrients and the mechanisms of their assimilation. In the present review, an attempt is made to do this, borrowing information from the physiology of bacteria, fungi, and higher plants where they augment observations on algae. In doing so, some erroneous suggestions are probable, but hopefully areas of needed research will be pointed out.

Inorganic nutrient uptake and deficiency in algae.

Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. Purification, prosthetic groups, and molecular properties.

Ammonia at concentrations above 1×10-5 M inhibits uptake of nitrate in the nitrogen-fixing blue-green alga, Anabaena cylindrica. This inhibition takes place both in the light and in the dark. The rate of nitrate uptake is stimulated by light. Addition of relatively high concentrations of nitrate (1–10 mM) reversibly inhibits ammonia uptake. FCCP, an uncoupler of phosphorylation, inhibits both nitrate and ammonia uptake. Ammonia may inhibit nitrate uptake by reducing the supply of energy (ATP) for active nitrate transport.

Inhibition of nitrate uptake by ammonia in a blue-green alga, Anabaena cylindrica

Allophycocyanins were purified from diverse cyanobacteria and one rhodophytan alga (Cyanidium caldarium). The native proteins are trimeric molecules with the structure (αβ)3. Representative native allophycocyanins and their α and β subunits were characterized with respect to molecular weight, amino acid composition, isoelectric point, absorption and fluorescence spectra and immunological properties. All of the allophycocyanins studied were strikingly similar with respect to each of these properties.

Physico-chemical and immunological properties of allophycocyanins.

A nitrate reductase from the thermophilic acidophilic alga, Cyanidium caldarium, was studied. The enzyme utilises the reduced forms of benzyl viologen and flavins as well as both NADPH2 and NADH2 as electron donors to reduce nitrate.

Studies on nitrate reductase from Cyanidium caldarium

A latent nitrate reductase from a thermophilic alga

The growth of Cyanidium caldarium on nitrate and ammonia as nitrogen sources was studied at different temperatures from 21 to 54°C.

Comparative growth of the thermal algae Cyanidium caldarium on nitrate and ammonia at different temperatures.

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Studies on nitrate reductase from Cyanidium caldarium

A latent nitrate reductase from a thermophilic alga

Comparative growth of the thermal algae Cyanidium caldarium on nitrate and ammonia at different temperatures.