Artificial metalloenzymes: the powerful alliance between protein scaffolds and organometallic catalysts

Benjamin Large; Natalia Baranska; Rosalind Booth; Keith Sanderson Wilson; Anne-Kathrin Duhme-Klair

doi:10.1016/j.cogsc.2020.100420

Artificial metalloenzymes: the powerful alliance between protein scaffolds and organometallic catalysts

Benjamin Large, Natalia Baranska, Rosalind Booth, Keith Sanderson Wilson, Anne-Kathrin Duhme-Klair

Chemistry

Research output: Contribution to journal › Review article › peer-review

Abstract

In recent years, substantial advances have been made in the development of artificial metalloenzymes. These hybrid bioinorganic catalysts have seen their selectivity improved through techniques including site-directed and site-saturation mutagenesis and directed evolution. Their scope has been expanded by the introduction of various abiological metal catalysts, the development of new anchoring strategies and new designs to enhance their reusability by conceiving modular and reversible assemblies. This review highlights a selection of the most significant advances made in the last two years and their contribution to the development of a more sustainable chemistry

Original language	English
Article number	100420
Number of pages	7
Journal	Current Opinion in Green and Sustainable Chemistry
Volume	28
Early online date	1 Dec 2020
DOIs	https://doi.org/10.1016/j.cogsc.2020.100420
Publication status	Published - 1 Apr 2021

Bibliographical note

This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy.

Access to Document

10.1016/j.cogsc.2020.100420

Green ArMs Accepted Author Manuscript
This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy.
Accepted author manuscript, 1.47 MBLicence: CC BY-NC-ND

2 Invited talk
1 Conference

Faraday Discussion Meeting Harnessing Non Covalent Interactions
Duhme-Klair, A.-K. (Committee member)
12 Apr 2023 → 14 Apr 2023
Activity: Participating in or organising an event › Conference
Iron on the move: using siderophores to deliver catalysts and antimicrobials (Osaka University, Japan)
Duhme-Klair, A.-K. (Invited speaker)
5 Dec 2022
Activity: Talk or presentation › Invited talk
Exploiting siderophores in the development of antimicrobials and artificial enzymes
Duhme-Klair, A.-K. (Keynote/plenary speaker)
21 May 2021
Activity: Talk or presentation › Invited talk

2 Finished

Redox-reversible artificial metalloenzymes
DUHME-KLAIR, A. (Principal investigator), JOHNSON, S. D. (Co-investigator) & WILSON, K. S. (Co-investigator)
27/01/20 → 31/10/23
Project: Research project (funded) › Research
Siderophores as anchors in artificial metalloenzymes
DUHME-KLAIR, A. (Principal investigator) & WILSON, K. S. (Co-investigator)
EPSRC
31/12/14 → 30/12/17
Project: Research project (funded) › Research

Cite this

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title = "Artificial metalloenzymes: the powerful alliance between protein scaffolds and organometallic catalysts",

abstract = "In recent years, substantial advances have been made in the development of artificial metalloenzymes. These hybrid bioinorganic catalysts have seen their selectivity improved through techniques including site-directed and site-saturation mutagenesis and directed evolution. Their scope has been expanded by the introduction of various abiological metal catalysts, the development of new anchoring strategies and new designs to enhance their reusability by conceiving modular and reversible assemblies. This review highlights a selection of the most significant advances made in the last two years and their contribution to the development of a more sustainable chemistry",

author = "Benjamin Large and Natalia Baranska and Rosalind Booth and Wilson, {Keith Sanderson} and Anne-Kathrin Duhme-Klair",

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AU - Large, Benjamin

AU - Baranska, Natalia

AU - Booth, Rosalind

AU - Wilson, Keith Sanderson

AU - Duhme-Klair, Anne-Kathrin

N1 - This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy.

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N2 - In recent years, substantial advances have been made in the development of artificial metalloenzymes. These hybrid bioinorganic catalysts have seen their selectivity improved through techniques including site-directed and site-saturation mutagenesis and directed evolution. Their scope has been expanded by the introduction of various abiological metal catalysts, the development of new anchoring strategies and new designs to enhance their reusability by conceiving modular and reversible assemblies. This review highlights a selection of the most significant advances made in the last two years and their contribution to the development of a more sustainable chemistry

AB - In recent years, substantial advances have been made in the development of artificial metalloenzymes. These hybrid bioinorganic catalysts have seen their selectivity improved through techniques including site-directed and site-saturation mutagenesis and directed evolution. Their scope has been expanded by the introduction of various abiological metal catalysts, the development of new anchoring strategies and new designs to enhance their reusability by conceiving modular and reversible assemblies. This review highlights a selection of the most significant advances made in the last two years and their contribution to the development of a more sustainable chemistry

U2 - 10.1016/j.cogsc.2020.100420

DO - 10.1016/j.cogsc.2020.100420

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JO - Current Opinion in Green and Sustainable Chemistry

JF - Current Opinion in Green and Sustainable Chemistry

M1 - 100420

ER -

Artificial metalloenzymes: the powerful alliance between protein scaffolds and organometallic catalysts

Abstract

Bibliographical note

Access to Document

Activities

Faraday Discussion Meeting Harnessing Non Covalent Interactions

Iron on the move: using siderophores to deliver catalysts and antimicrobials (Osaka University, Japan)

Exploiting siderophores in the development of antimicrobials and artificial enzymes

Projects

Redox-reversible artificial metalloenzymes

Siderophores as anchors in artificial metalloenzymes

Cite this