Walton, Paul H. orcid.org/0000-0002-1152-1480, Davies, Gideon J. orcid.org/0000-0002-7343-776X, Diaz, Daniel E. et al. (1 more author) (2023) The histidine brace:nature's copper alternative to haem? FEBS Letters. pp. 485-494. ISSN 0014-5793
Abstract
The copper histidine brace is a structural unit in metalloproteins (Proc Natl Acad Sci USA 2011, 108, 15079). It consists of a copper ion chelated by the NH2 and π-N atom of an N-terminal histidine, and the τ-N atom of a further histidine, in an overall T-shaped coordination geometry (Nat Catal 2018, 1, 571). Like haem-containing proteins, histidine-brace-containing proteins have peroxygenase and/or oxygenase activity, where the substrates are notable for resistance to oxidation, for example, lytic polysaccharide monooxygenases (LPMOs). Moreover, the histidine brace is an invariant unit around which different protein structures exert different activities. Given the similarities in the diversity of function of proteins that contain either the copper histidine brace or haem, the question arises as to whether the functions of histidine brace-containing proteins duplicate those containing haem groups.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2023 The Authors. Funding Information: GJD and PHW thank the Biotechnology and Biological Sciences Research Council for support (BB/R007705/1, BB/V0040069/1). |
Keywords: | copper,haem,histidine brace,LPMOs |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/R007705/1 BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/V0040069/1 THE ROYAL SOCIETY RSRP\R\210004 |
Depositing User: | Pure (York) |
Date Deposited: | 22 Feb 2023 11:10 |
Last Modified: | 05 Mar 2025 00:08 |
Published Version: | https://doi.org/10.1002/1873-3468.14579 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1002/1873-3468.14579 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:196693 |
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