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Inhibition by acetylene of conventional hydrogenase in nitrogen-fixing bacteria

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Abstract

ONE of the earliest observations associated with nitrogen fixation was that all nitrogen-fixing organisms contained hydrogenase and nitrogenase1. We show here that acetylene, which is widely used as a substrate for nitrogenase, inhibits conventional hydrogenase activity and thus prevents the uptake of H2 formed by nitrogenase in the presence of CO. Our evidence also suggests that azotobacter nitrogenase forms H2 in vivo and that hydrogenase reoxidises this H2 to provide reducing power for metabolism.

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Authors and Affiliations

  1. A. R. C. Unit of Nitrogen Fixation, The University of Sussex, Palmer, Brighton, Sussex, BN1 9QJ, UK

    LINDA A. SMITH, SUSAN HILL & M. G. YATES

Authors
  1. LINDA A. SMITH
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  2. SUSAN HILL
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  3. M. G. YATES
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SMITH, L., HILL, S. & YATES, M. Inhibition by acetylene of conventional hydrogenase in nitrogen-fixing bacteria. Nature 262, 209–210 (1976). https://doi.org/10.1038/262209a0

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