These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A model of nitrogenase active-centre and mechanism of nitrogenase catalysis.
    Journal: Sci Sin; 1976; 19(4):460-74. PubMed ID: 982022.
    Abstract:
    Based upon the known reactions of nitrogenase and the principles of coordination catalysis, a model of nitrogenase active-centre is proposed. An octa-atomic cluster, Fe2S2-Mo2O2, of pseudo-cubane-type structure is supposed to form a coupled twin of trinuclear (2Mo-1Fe) active-centre, which also catalyzes the reduction of H+ to H2. With this model, mechanisms of all the known nitrogenase-catalyzed reactions are explained, together with the non-inhibition of the hydrogen-evolution reaction by CO, and the mixed character of inhibition of other nitrogenase-catalyzed reactions. Electron transport by 2-stepped ATP-driving with some electron back-flow is shown to give a reasonable explanation for the observed ATP/2e- ratio and for the reductant-independent ATP hydrolysis catalyzed by nitrogenase. The close analogy between electron transport by 2-stepped ATP-driving in nitrogenase catalysis and electron transport by 2-stepped photo-driving in photosynthesis by green plants in illustrated.
    [Abstract] [Full Text] [Related] [New Search]