Abstract
Work in our laboratories has involved the use of genetic, biochemical, and biophysical approaches to analyze the assembly and catalytic mechanism of nitrogenase. Azotobacter vinelandii has been used for these studies because it produces copious amounts of the catalytic components of nitrogenase - the Fe protein and the MoFe protein - and because it is amenable to sophisticated genetic manipulation. Groundwork in our laboratories, and in the laboratory of Paul Bishop, involved the isolation and nucleotide sequence analysis of all, or most, of the A. vinelandii genes directly involved in nitrogenase catalysis. Work in Bishop’s laboratory ultimately led to the remarkable discovery and characterization of two “alternative” nitrogenases, a Vanadium-dependent and Iron-only nitrogenase. We, on the other hand, have concentrated on the characterization of the “traditional” Molybdenum-dependent enzyme. It is worth noting that some - but not all - of the gene products required for maturation of the Mo-dependent enzyme are also required for maturation of the alternative nitrogenases (Kennedy, Dean, 1992). How the expression of these various genes is controlled to permit the accumulation of the appropriate form of nitrogenase -under the appropriate conditions - is a fascinating question currently under study in several laboratories.
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© 1998 Springer Science+Business Media Dordrecht
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Dean, D.R. et al. (1998). Activation of Iron and Sulfur for Nitrogenase Metallocluster Formation. In: Elmerich, C., Kondorosi, A., Newton, W.E. (eds) Biological Nitrogen Fixation for the 21st Century. Current Plant Science and Biotechnology in Agriculture, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5159-7_6
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DOI: https://doi.org/10.1007/978-94-011-5159-7_6
Publisher Name: Springer, Dordrecht
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