Abstract
THE molybdenum-containing enzyme nitrogenase1 catalyses the ATP-dependent six-electron reduction of dinitrogen (N2) to NH3. Previous attempts to detect partially reduced nitrogen intermediates, both enzyme-bound and free in solution, have failed2,3. We report here the first detection of an enzyme-bound dinitrogen intermediate, which is only present when the enzyme is reducing N2 and which on both acid and alkali hydrolysis yields hydrazine (N2H4). This dinitrogen intermediate need not be N2H4, because the chemistry of Mo and W dinitrogen complexes (see below) suggests that other enzyme-bound dinitrogen-hydride intermediate species could undergo non-enzymatic hydrolysis on acid and alkali quenching of the enzyme reaction to give N2H4.
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THORNELEY, R., EADY, R. & LOWE, D. Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate. Nature 272, 557–558 (1978). https://doi.org/10.1038/272557a0
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DOI: https://doi.org/10.1038/272557a0
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