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Iron-containing ureases
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DOI：10.1016/j.ccr.2021.214190.png)
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摘要
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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.
Keyword:
Urease
Dinuclear iron
Resonance Raman spectroscopy
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23.5
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