By the same authors

From the same journal

Redox-switchable siderophore anchor enables reversible artificial metalloenzyme assembly

Research output: Contribution to journalArticle

Full text download(s)

Published copy (DOI)

Author(s)

Department/unit(s)

Publication details

JournalNature Catalysis
DateAccepted/In press - 6 Jul 2018
DateE-pub ahead of print - 20 Aug 2018
DatePublished (current) - 1 Sep 2018
Issue number9
Volume1
Number of pages9
Pages (from-to)680-688
Early online date20/08/18
Original languageEnglish

Abstract

Artificial metalloenzymes that contain protein-anchored synthetic catalysts are attracting increasing interest. An exciting, but still unrealized advantage of non-covalent anchoring is its potential for reversibility and thus component recycling. Here we present a siderophore–protein combination that enables strong but redox-reversible catalyst anchoring, as exemplified by an artificial transfer hydrogenase (ATHase). By linking the iron(iii)-binding siderophore azotochelin to an iridium-containing imine-reduction catalyst that produces racemic product in the absence of the protein CeuE, but a reproducible enantiomeric excess if protein bound, the assembly and reductively triggered disassembly of the ATHase was achieved. The crystal structure of the ATHase identified the residues involved in high-affinity binding and enantioselectivity. While in the presence of iron(iii), the azotochelin-based anchor binds CeuE with high affinity, and the reduction of the coordinated iron(iii) to iron(ii) triggers its dissociation from the protein. Thus, the assembly of the artificial enzyme can be controlled via the iron oxidation state.

Bibliographical note

© 2018, Springer Nature. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details

Activities

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations