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Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate

Nature volume 272, pages 557558 (06 April 1978) | Download Citation

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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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Author information

Affiliations

  1. ARC Unit of Nitrogen Fixation, University of Sussex, Brighton BN1 9QJ, UK

    • ROGER N. F. THORNELEY
    • , ROBERT R. EADY
    •  & DAVID J. LOWE

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https://doi.org/10.1038/272557a0

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