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Updated: Oct 15, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Environment and coordination of FeMo-co in the nitrogenase metallochaperone NafY
Aaron H Phillips1, Jose A Hernandez2,3, Lucía Payá-Tormo4
1St. Jude Children's Research Hospital Memphis TN 38105 USA.
Abstract:
In nitrogenase biosynthesis, the iron-molybdenum cofactor (FeMo-co) is externally assembled at scaffold proteins and delivered to the NifDK nitrogenase component by the NafY metallochaperone. Here we have used nuclear magnetic resonance, molecular dynamics, and functional analysis to elucidate the environment and coordination of FeMo-co in NafY. H121 stands as the key FeMo-co ligand. Regions near FeMo-co diverge from H121 and include the η1, α1, α2 helical lobe and a narrow path between H121 and C196.
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