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

Alex Henrique Miller; Sean Thompson; Lena Blagova; Keith Sanderson Wilson; Gideon James Grogan; Anne-Kathrin Duhme-Klair

doi:10.1039/D4CC01158A

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

Alex Henrique Miller^*, Sean Thompson, Lena Blagova, Keith Sanderson Wilson, Gideon James Grogan, Anne-Kathrin Duhme-Klair^*

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Article › peer-review

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 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.

Original language	English
Number of pages	4
Journal	Chemical communications
Early online date	29 Apr 2024
DOIs	https://doi.org/10.1039/D4CC01158A
Publication status	E-pub ahead of print - 29 Apr 2024

Bibliographical note

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10.1039/D4CC01158ALicence: CC BY

d4cc01158a
© The Royal Society of Chemistry 2024
Final published version, 2.95 MBLicence: CC BY

2 Finished

21ENGBIO In Cell Assembly of Artificial Imine Reductases for Applications in Whole-Cell Catalysis
Duhme-Klair, A., Grogan, G. J., O'Toole, P. J. & Wilson, K. S.
BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL)
15/02/23 → 14/02/24
Project: Research project (funded) › Research
Redox-reversible artificial metalloenzymes
Duhme-Klair, A., Johnson, S. D. & Wilson, K. S.
27/01/20 → 31/10/23
Project: Research project (funded) › Research

Dataset associated with publication: Kinetic and structural analysis of redox-reversible artificial imine reductases
Miller, A. H. (Data Collector), Martins, I. (Contributor) & Duhme-Klair, A. (Creator), University of York, 29 Jul 2024
DOI: 10.15124/65fe7181-d559-4573-a062-40e064929706
Dataset

Cite this

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

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 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.",

author = "Miller, {Alex Henrique} and Sean Thompson and Lena Blagova and Wilson, {Keith Sanderson} and Grogan, {Gideon James} and Anne-Kathrin Duhme-Klair",

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AU - Miller, Alex Henrique

AU - Thompson, Sean

AU - Blagova, Lena

AU - Wilson, Keith Sanderson

AU - Grogan, Gideon James

AU - Duhme-Klair, Anne-Kathrin

PY - 2024/4/29

Y1 - 2024/4/29

N2 - 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 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.

AB - 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 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.

U2 - 10.1039/D4CC01158A

DO - 10.1039/D4CC01158A

M3 - Article

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SN - 1359-7345

JO - Chemical communications

JF - Chemical communications

ER -

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

Abstract

Bibliographical note

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Projects

21ENGBIO In Cell Assembly of Artificial Imine Reductases for Applications in Whole-Cell Catalysis

Redox-reversible artificial metalloenzymes

Datasets

Dataset associated with publication: Kinetic and structural analysis of redox-reversible artificial imine reductases

Cite this