español    español

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.


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

Centre for Plant Biotechnology and Genomics UPM – INIA Parque Científico y Tecnológico de la U.P.M. Campus de Montegancedo
Autopista M-40, Km 38 - 28223 Pozuelo de Alarcón (Madrid) Tel.: +34 91 0679100 ext. 79100 Fax: +34 91 7157721. Location and Contact

Síguenos en: