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Abstract
Annual Review of Microbiology
Vol. 62: 93-111 (Volume publication date October 2008)
(doi:10.1146/annurev.micro.62.081307.162737)
First published online as a Review in Advance on April 22, 2008
Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase

Luis M. Rubio1 and ­Paul W. Ludden2­
1Department of Plant and Microbial Biology, University of California, Berkeley, California 94720; email:
2Office of the Provost, Southern Methodist University, Dallas, Texas 75275; email:

The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum nitrogenase, is one of the most complex metal cofactors known to date. During the past several years, an intensive effort has been made to purify the proteins involved in FeMo-co synthesis and incorporation into nitrogenase. This effort is starting to provide insights into the structures of the FeMo-co biosynthetic intermediates and into the biochemical details of FeMo-co synthesis.

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Authors:
Luis M. Rubio
Paul W. Ludden
Keywords:
nitrogen fixation
nif
FeMo-co
iron-sulfur
NifDK
MoFe protein

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