Horch, Marius (2019) Rational redox tuning of transition metal sites:Learning from superoxide reductase. Chemical Communications. pp. 9148-9151. ISSN 1364-548X
Abstract
Using superoxide reductase as a model system, a computational approach reveals how histidine tautomerism tunes the redox properties of metalloenzymes to enable their catalytic function. Inspired by these experimentally inaccessible insights, non-canonical histidine congeners are introduced as new versatile tools for the rational engineering of biological transition metal sites.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | 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. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 14 Aug 2019 09:20 |
Last Modified: | 07 Feb 2025 00:25 |
Published Version: | https://doi.org/10.1039/c9cc04004h |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.1039/c9cc04004h |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:149707 |
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