Enzyme Control Over Ferric Iron Magnetostructural Properties

Fe3+ complexes in aqueous solution can exist as discrete mononuclear species or multinuclear magnetically coupled species. Stimuli‐driven change to Fe3+ speciation represents a powerful mechanistic basis for magnetic resonance sensor technology, but ligand design strategies to exert precision contro...

Full description

Saved in:
Bibliographic Details
Published in:Angewandte Chemie 2022-01, Vol.134 (3), p.n/a
Main Authors: Wang, Huan, Cleary, Michael B., Lewis, Luke C., Bacon, Jeffrey W., Caravan, Peter, Shafaat, Hannah S., Gale, Eric M.
Format: Article
Language:English
Subjects:
Antiferromagnetism
Aqueous solutions
Bioresponsive
Carboxylesterase
Chemistry
Coordination compounds
Imaging
Iron
Ligands
Magnetic properties
Magnetic resonance
Sensors
Speciation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Fe3+ complexes in aqueous solution can exist as discrete mononuclear species or multinuclear magnetically coupled species. Stimuli‐driven change to Fe3+ speciation represents a powerful mechanistic basis for magnetic resonance sensor technology, but ligand design strategies to exert precision control of aqueous Fe3+ magnetostructural properties are entirely underexplored. In pursuit of this objective, we rationally designed a ligand to strongly favor a dinuclear μ‐oxo‐bridged and antiferromagnetically coupled complex, but which undergoes carboxylesterase mediated transformation to a mononuclear high‐spin Fe3+ chelate resulting in substantial T1‐relaxivity increase. The data communicated demonstrate proof of concept for a novel and effective strategy to exert biochemical control over aqueous Fe3+ magnetic, structural, and relaxometric properties. We introduce a first‐in‐class stimuli responsive Fe3+ complex that is switched between discrete antiferromagnetically coupled and high‐spin paramagnetic species through the action of a carboxylesterase enzyme. We also demonstrate how enzyme‐mediated switching of Fe3+ magnetic properties offers a mechanistic foundation for new bioresponsive magnetic resonance sensor technology.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.202114019