Issue 5, 2021

Environment and coordination of FeMo–co in the nitrogenase metallochaperone NafY

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.

Graphical abstract: Environment and coordination of FeMo–co in the nitrogenase metallochaperone NafY

Supplementary files

Article information

Article type
Communication
Submitted
21 4 2021
Accepted
27 7 2021
First published
28 7 2021
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2021,2, 1462-1465

Environment and coordination of FeMo–co in the nitrogenase metallochaperone NafY

A. H. Phillips, J. A. Hernandez, L. Payá-Tormo, S. Burén, B. Cuevas-Zuviría, L. F. Pacios, J. G. Pelton, D. E. Wemmer and L. M. Rubio, RSC Chem. Biol., 2021, 2, 1462 DOI: 10.1039/D1CB00086A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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