Iron-containing ureases

Conventional ureases possess dinuclear nickel active sites that are oxygen-stable and require a set of accessory proteins for metallocenter biosynthesis. By contrast, oxygen-labile ureases have active sites containing dual ferrous ions and lack a requirement for maturation proteins. The structures of the two types of urease are remarkably similar, with an active site architecture that includes two imidazoles and a carboxylate ligand coordinated to one metal, two imidazoles coordinated to the second metal, and a metal-bridging carbamylated lysine ligand. The electronic spectrum of the diferric form of the enzyme resembles that of methemerythrin. Resonance Raman spectroscopic analyses confirm the presence of a mu-oxo ligand and indicate the presence of one or more terminal solvent ligands. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

Conventional ureases and oxygen-labile ureases have similar structures, but differ significantly in their active sites and requirements for accessory proteins.