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PubMed1987

Physiological conditions for nitrogen fixation in a unicellular marine cyanobacterium, Synechococcus sp. strain SF1.

A marine, unicellular, nitrogen-fixing cyanobacterium was isolated from the blades of a brown alga, Sargassum fluitans. This unicellular cyanobacterium, identified as Synechococcus sp. strain SF1, is capable of photoautotrophic growth with bicarbonate as the sole carbon source and dinitrogen as the sole nitrogen source. Among the organic carbon compounds tested, glucose and sucrose supported growth. Of the nitrogen compounds tested, with bicarbonate serving as the carbon source, both ammonia and nitrate produced the highest growth rates. Most amino acids failed to support growth when present as sole sources of nitrogen. Nitrogenase activity in Synechococcus sp. strain SF1 was induced after depletion of ammonia from the medium. This activity required the photosynthetic utilization of bicarbonate, but pyruvate and hydrogen gas were also effective sources of reductant for nitrogenase activity. Glucose, fructose, and sucrose also supported nitrogenase activity but to a lesser extent. Optimum light intensity for nitrogenase activity was found to be 70 microE/m2 per s, while the optimum oxygen concentration in the gas phase for nitrogenase activity was about 1%. A hydrogenase activity was coinduced with nitrogenase activity. It is proposed that this light- and oxygen-insensitive hydrogenase functions in recycling the hydrogen produced by nitrogenase under microaerobic conditions.

Ammonia↗
PubMed1984

Hydrogen oxidation and nitrogen fixation in rhizobia, with special attention focused on strain ORS 571.

In this survey we describe the influence of hydrogen oxidation on the physiology of Rhizobium ORS 571. The presence of hydrogen is required for the synthesis of hydrogenase. Carbon substrates do not repress the synthesis of hydrogenase. The respiratory system contains cytrochromes of the b- and c-type. Cytochrome alpha 600 is present after growth at high oxygen tensions. The nature of the terminal oxidases functioning at low oxygen tensions has not been established yet----H+/O values with endogenous substrates are between 6 and 7. The results show the presence of two phosphorylation sites: site 1 (ATP/2e = 1.0) and site 2(ATP/2e = 1.33). By measuring molar growth yields it has been demonstrated that carbon-limited, nitrogen-fixing cultures obtain additional ATP from hydrogen oxidation, and that site 2 of oxidative phosphorylation is passed during hydrogen oxidation. A method is described to calculate ATP/N2 values (the total amount of ATP used by nitrogenase during the fixation of 1 mol N2) and H2/N2 ratios (mol hydrogen formed per mol N2 fixed) in aerobic organisms. For Rhizobium ORS 571 the ATP/N2 value is about 40 and the H2/N2 ratio is between 5 and 7.5. Cells obtained from oxygen-limited nitrogen-fixing cultures contain 30-40% poly-beta-hydroxybutyrate, which explains the high molar growth yields found. Hydrogen has not been detected in the effluent gas of these cultures, which may point to reoxidation of the hydrogen formed at nitrogen fixation. Calculations show that the effect of hydrogen reoxidation on the efficiency of nitrogen fixation (g N fixed X mol-1 substrate converted) is not very large and that the actual H2/N2 ratio is of much more importance. After addition of hydrogen to succinate-limited, ammonia-assimilating cultures, an initial increase of the Ysuccinate value (g dry wt X mol-1 succinate) is followed by a gradual decrease. This is accompanied by a large decrease of the YO2 value, and an increased permeability of the cytoplasmic membrane to protons. The results may be explained by a transition of the culture from an energy-limited state to a carbon-limited state.

Adenosine Triphosphate↗