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A small metallochaperone balances transfer and protection of the labile iron-molybdenum cofactor of nitrogenase

Cell function requires metals that participate as metalloprotein prosthetic groups. Metallochaperones control metal reactivity and metal cluster integrity in cellular metal trafficking networks. One example is that of NafY and the iron-molybdenum cofactor of nitrogenase. Here we investigate their association by nuclear magnetic resonance, molecular dynamics, and functional analysis. Understanding this complex is crucial in the biotechnology context of generating plants capable of using atmospheric nitrogen.

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Original Paper:

Phillips, A.H., Hernandez, J.A., Payá-Tormo, L., Burén, S., Cuevas-Zuviría, B., Pacios, L.F., Pelton, J.G., Wemmer, D.E., Rubio, L.M. 2021. Environment and coordination of FeMo–co in the nitrogenase metallochaperone NafY. RSC Chemical Biology. DOI: 10.1039/D1CB00086A

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