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Abstract

Biological nitrogen fixation, an energy intensive process, is subject to several control processes in the cell (Brill, 1975; Ludden and Burris, 1976; Carithers and Yoch, 1979; Shanmugam and Hennecke, 1979). These include both genetic regulatory mechanisms and protein modification (in some organisms like Rhodospirilium rubrum). Addition of either NH4 + or O2 to a nitrogen-fixing culture immediately leads to repression of nitrogenase biosynthesis. In Klebsiella pneumoniae, nitrogenase synthesis is also regulated by growth temperature (Hennecke and Shanmugam, 1979). Nitrogenase is undetectable at elevated temperatures (> 37 C) under growth conditions that allow the production of nitrogenase at permissive temperatures. Although NH4 + and high temperature (39 C) repress nitrogenase biosynthesis, they have no detectable effect on preformed nitrogenase protein and catalytic activity. Ammonium ion mediated regulation of nitrogenase (NH4 +-control) is believed to be mediated through the assimilation of NH4 + to the level of organic compounds. The mechanism by which temperature affects the production of nitrogenase is unknown. These two control systems will not be discussed in this communication, with emphasis here on the role of O2 as a modulator of synthesis of nitrogenase. The term ‘redox control’ used in the title refers to the fact that molecular oxygen (and other compounds such as nitrate) have the dual role as terminal electron acceptors as well as genetic modulators of cellular activity. A lucid description of the role of O2 as a biochemical regulator is presented by Schlegel and coworkers in this volume.

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© 1981 Plenum Press, New York

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Shanmugam, K.T., Lim, S.T., Hom, S.S.M., Scott, D.B., Hennecke, H. (1981). “Redox Control” of Nitrogen Fixation: An Overview. In: Lyons, J.M., Valentine, R.C., Phillips, D.A., Rains, D.W., Huffaker, R.C. (eds) Genetic Engineering of Symbiotic Nitrogen Fixation and Conservation of Fixed Nitrogen. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3953-3_9

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  • DOI: https://doi.org/10.1007/978-1-4684-3953-3_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3955-7

  • Online ISBN: 978-1-4684-3953-3

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