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: Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase.
    Author: Igarashi RY, Seefeldt LC.
    Journal: Crit Rev Biochem Mol Biol; 2003; 38(4):351-84. PubMed ID: 14551236.
    Abstract:
    This review focuses on recent developments elucidating the mechanism of the Mo-dependent nitrogenase. This enzyme, responsible for the majority of biological nitrogen fixation, is composed of two component proteins called the MoFe protein and the Fe protein. Recent progress in understanding the mechanism of this enzyme has focused on elucidating the structures of the active site metal clusters and of the proteins, understanding substrate interactions with the active site, defining the flow of electron transfer between the metal clusters, and defining the various roles of MgATP hydrolysis.
    [Abstract] [Full Text] [Related] [New Search]