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

Chem Commun (Camb). 2024 May 21;60(42):5490-5493. doi: 10.1039/d4cc01158a.

Abstract

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.

MeSH terms

  • Biocatalysis
  • Catalysis
  • Cross-Linking Reagents / chemistry
  • Iron / chemistry
  • Metalloproteins / chemistry
  • Metalloproteins / metabolism
  • Oxidation-Reduction*
  • Siderophores* / chemistry
  • Stereoisomerism