Abstract
Nitrogenase is the enzyme which converts dinitrogen to ammonia and is responsible for the 122 million metric tonnes of nitrogen which is estimated to be fixed annually by micro-organisms (Burris, 1980). The ability to fix dinitrogen is currently restricted to prokaryotes but genetic manipulation may eventually enable organelles such as chloroplasts or mitochondria to fix nitrogen in higher organisms such as plants. Nitrogenase is present in both obligate (e.g. Clostridium pasteurianum, Cp) and facultative (e.g. Klebsiella pneumoniae, Kp) anaerobes, obligate aerobes (e.g. Azotobacter vinelandii, Av), photosynthetic bacteria (e.g. Rhodospirillum rubrum, Rr), cyanobacteria (e.g. Anabaena cylindrica, Ab) and the bacteria which form both casual (e.g. Azospirillum brasilense, Azb) and symbiotic (e.g. Rhizobium japonicum, Rj) associations with plant root systems. This list is not exhaustive and the reader is referred to Postgate (1981) and Starr et al. (1981) for authoritative discussions of the microbiology of nitrogen fixation. The list above does serve to introduce the shorthand notation that will be used in this chapter for the two proteins that comprise nitrogenase. The addition of the number 1 or 2 to the code designates either the molybdenum iron (MoFe) protein (e.g. Kp1) or the iron (Fe) protein (e.g. Kp2) of for example, the nitrogenase from K. pneumoniae.
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Lowe, D.J., Thorneley, R.N.F., Smith, B.E. (1985). Nitrogenase. In: Harrison, P.M. (eds) Metalloproteins. Topics in Molecular and Structural Biology. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06372-7_6
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DOI: https://doi.org/10.1007/978-1-349-06372-7_6
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