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Enhanced rare-earth separation with a metal-sensitive lanmodulin dimer
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Journal Article
Enhanced rare-earth separation with a metal-sensitive lanmodulin dimer
2023
Overview
Technologically critical rare-earth elements are notoriously difficult to separate, owing to their subtle differences in ionic radius and coordination number
1
–
3
. The natural lanthanide-binding protein lanmodulin (LanM)
4
,
5
is a sustainable alternative to conventional solvent-extraction-based separation
6
. 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.
A study biochemically and structurally characterizes a lanmodulin from
Hansschlegelia quercus
with an oligomeric state sensitive to rare-earth ionic radius.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Dimers
/ Dysprosium - isolation & purification
/ Earth
/ Hands
/ Humanities and Social Sciences
/ Lanthanoid Series Elements - chemistry
/ Lanthanoid Series Elements - isolation & purification
/ Neodymium - isolation & purification
/ Protein Structure, Quaternary
/ Proteins
/ Science
