Summary
The influence of amino acids, ammonium chloride and oxygen on the nitrogenase activities of Azospirillum spp. was examined. In the presence of glutamate, aspartate, histidine or proline nitrogen fixation in A. brasilense strains was only slightly reduced, whereas in A. lipoferum and A. amazonense strains these amino acids almost completely abolished nitrogen fixation. Differences in the levels of ammonium assimilatory enzymes were found. After the addition of ammonium chloride, nitrogenase activity was completely inhibited in A. brasilense and A. lipoferum, but only partially inhibited in A. amazonense. In A. brasilense and A. lipoferum a covalent modification of the Fe protein of nitrogenase was involved in the “MATHTYPE switch off” as in R. rubrum. In A. amazonense no modified subunit of the Fe protein was found. Oxygen inhibited the nitrogenase activity of A. brasilense most effectively, whereas in A. amazonense the nitrogenase activity was remarkably oxygen tolerant. After the cells were exposed to inhibitory oxygen concentrations, the nitrogenase activity of all three species was recovered at a low pO2 No dification of the Fe protein occurred during the “oxygen-switch off”. However, under anaerobic conditions, the Fe protein of A. brasilense and A. lipoferum was modified.
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Hartmann, A., Fu, HA., Song, SD., Burris, R.H. (1985). Comparison of Nitrogenase Regulation in A. Brasilense, A. Lipoferum, and A. Amazonense. In: Klingmüller, W. (eds) Azospirillum III. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70791-9_12
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DOI: https://doi.org/10.1007/978-3-642-70791-9_12
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