Nitrogenase, a bacterial enzyme responsible for biological nitrogen fixation, has in its catalytic site a complex set of iron, molybdenum, carbon and sulfur atoms, called FeMo-co. Biosynthesis of this cofactor takes place outside the enzyme and involves the activities of a number of nitrogen-fixing gene (NIF) products. Nif proteins are required to provide the atomic constituents of FeMo-co and the cofactor assembly molecular scaffolds to facilitate the transfer of FeMo-co biosynthetic intermediates to the nitrogenase. Despite this apparent complexity, three proteins - NifB, NifEN and NifH - are involved in this chemistry. This observation has led to a substantial simplification of the nitrogenase biosynthetic pathway, and its integration into plants. This presentation showed how recent advances in our understanding of nitrogenase biosynthesis offer new perspectives on this ambitious agronomic goal.
Amphithéâtre Maurice Halbwachs, Site Marcelin Berthelot
Open to all, subject to availability
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Audio recording
References
Rubio L.M. and Ludden P.W., "Biosynthesis of the iron-molybdenum cofactor of nitrogenase", Annu. Rev. Microbiol, 62, 93-111(2008).
Curatti L et al, "In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins", Proc. Natl. Acad. Sci. U.S.A., 104, 17626-17631(2007).
Beatty P.H. and Good A.G., "Future prospects for cereals that fix nitrogen", Science, 333, 416-417 (2011).
Speaker(s)
Luis Rubio
Professor, Technical University Madrid, (Spain)