Redox-reversible siderophore-based catalyst anchoring within cross-linked artificial metalloenzyme aggregates enables enantioselectivity switching

The immobilisation of artificial metalloenzymes (ArMs) holds promise for the implementation of new biocatalytic reactions. We present the synthesis of cross-linked artificial metalloenzyme aggregates (CLArMAs) with excellent recyclability, as an alternative to carrier-based immobilisation strategies...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2024-05, Vol.6 (42), p.549-5493
Hauptverfasser: Miller, Alex H, Thompson, Seán A, Blagova, Elena V, Wilson, Keith S, Grogan, Gideon, Duhme-Klair, Anne-K
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container_end_page 5493
container_issue 42
container_start_page 549
container_title Chemical communications (Cambridge, England)
container_volume 6
creator Miller, Alex H
Thompson, Seán A
Blagova, Elena V
Wilson, Keith S
Grogan, Gideon
Duhme-Klair, Anne-K
description The immobilisation of artificial metalloenzymes (ArMs) holds promise for the implementation of new biocatalytic reactions. We present the synthesis of cross-linked artificial metalloenzyme aggregates (CLArMAs) with excellent recyclability, as an alternative to carrier-based immobilisation strategies. Furthermore, iron-siderophore supramolecular anchoring facilitates redox-triggered cofactor release, enabling CLArMAs to be recharged with alternative cofactors for diverse selectivity. The cross-linking of redox-reversible artificial metalloenzyme aggregates produces recyclable protein microparticles that enable catalyst replacement and hence catalyst-controlled enantioselectivity switching.
doi_str_mv 10.1039/d4cc01158a
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source Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
subjects Aggregates
Chemical synthesis
Chemistry
Crosslinking
Enantiomers
Immobilization
Recyclability
title Redox-reversible siderophore-based catalyst anchoring within cross-linked artificial metalloenzyme aggregates enables enantioselectivity switching
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