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Nature ; 618(7963): 87-93, 2023 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-37259003

RESUMEN

Technologically critical rare-earth elements are notoriously difficult to separate, owing to their subtle differences in ionic radius and coordination number1-3. The natural lanthanide-binding protein lanmodulin (LanM)4,5 is a sustainable alternative to conventional solvent-extraction-based separation6. Here we characterize a new LanM, from Hansschlegelia quercus (Hans-LanM), with an oligomeric state sensitive to rare-earth ionic radius, the lanthanum(III)-induced dimer being >100-fold tighter than the dysprosium(III)-induced dimer. X-ray crystal structures illustrate how picometre-scale differences in radius between lanthanum(III) and dysprosium(III) are propagated to Hans-LanM's quaternary structure through a carboxylate shift that rearranges a second-sphere hydrogen-bonding network. Comparison to the prototypal LanM from Methylorubrum extorquens reveals distinct metal coordination strategies, rationalizing Hans-LanM's greater selectivity within the rare-earth elements. Finally, structure-guided mutagenesis of a key residue at the Hans-LanM dimer interface modulates dimerization in solution and enables single-stage, column-based separation of a neodymium(III)/dysprosium(III) mixture to >98% individual element purities. This work showcases the natural diversity of selective lanthanide recognition motifs, and it reveals rare-earth-sensitive dimerization as a biological principle by which to tune the performance of biomolecule-based separation processes.


Asunto(s)
Proteínas Bacterianas , Elementos de la Serie de los Lantanoides , Lantano , Multimerización de Proteína , Disprosio/química , Disprosio/aislamiento & purificación , Iones/química , Elementos de la Serie de los Lantanoides/química , Elementos de la Serie de los Lantanoides/aislamiento & purificación , Lantano/química , Neodimio/química , Neodimio/aislamiento & purificación , Methylocystaceae , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Cristalografía por Rayos X , Estructura Cuaternaria de Proteína
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