So That's How It's Done--Maybe

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Science  04 Jul 2003:
Vol. 301, Issue 5629, pp. 55-56
DOI: 10.1126/science.1086678

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Many synthetic studies have aimed to mimic the nitrogen fixation by nitrogenase enzymes. Yandulov and Schrock now report a chemical cycle to reduce dinitrogen to ammonia based on a series of molybdenum complexes moving between oxidation states III and VI. In his Perspective, Leigh explains that these results make it appear more likely that molybdenum rather than iron is the site of dinitrogen reduction in conventional molybdenum nitrogenases. The assumption that molybdenum is at the active site of conventional molybdenum nitrogenases is consistent with recently published data on the role of homocitrate in dinitrogen reduction by nitrogenases, and with the discovery of a central light atom in the active-site cluster that seems to cast doubt on iron as the dinitrogen binding site.