dc.contributor.author |
Sullivan, Matthew P |
|
dc.contributor.author |
Cziferszky, Monika |
|
dc.contributor.author |
Tolbatov, Iogann |
|
dc.contributor.author |
Truong, Dianna |
|
dc.contributor.author |
Mercadante, Davide |
|
dc.contributor.author |
Re, Nazzareno |
|
dc.contributor.author |
Gust, Ronald |
|
dc.contributor.author |
Goldstone, David C |
|
dc.contributor.author |
Hartinger, Christian |
|
dc.coverage.spatial |
Germany |
|
dc.date.accessioned |
2021-08-09T23:38:25Z |
|
dc.date.available |
2021-08-09T23:38:25Z |
|
dc.date.issued |
2021-7 |
|
dc.identifier.citation |
Angewandte Chemie (International ed. in English) 60(36):19928-19932 Sep 2021 |
|
dc.identifier.issn |
1433-7851 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/55926 |
|
dc.description.abstract |
Metal complexes can be considered a 'paradigm of promiscuity' when it comes to their reactions with proteins. They often form adducts with a variety of donor atoms in an unselective manner. We have characterized the adducts formed between a series of isostructural N -heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry. Distinctive behavior for the metal compounds was observed with the more labile Ru and Rh complexes targeting a surface l-histidine moiety through cleavage of p- cymene or NHC co-ligands, respectively. In contrast, the more inert Os and Ir derivatives were detected in an electronegative binding pocket after undergoing ligand exchange of a chlorido ligand for an amino acid side chain. Computational studies supported the binding profiles and hinted at the role of the protein microenvironment for metal complexes eliciting selectivity for specific binding sites on the protein. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
Wiley |
|
dc.relation.ispartofseries |
Angewandte Chemie (International ed. in English) |
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dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights |
This is the peer reviewed version of the following article: Angewandte Chemie (International ed. in English) 60(36):19928-19932 Sep 2021, which has been published in final form at http://doi.org/10.1002/anie.202106906 This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.rights.uri |
https://authorservices.wiley.com/author-resources/Journal-Authors/licensing/self-archiving.html |
|
dc.subject |
Bioorganometallic chemistry |
|
dc.subject |
Metal-protein interactions |
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dc.subject |
N-Heterocyclic carbene complexes |
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dc.subject |
Protein crystallography |
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dc.subject |
Protein mass spectrometry |
|
dc.subject |
03 Chemical Sciences |
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dc.title |
Probing the Paradigm of Promiscuity for N-Heterocyclic Carbene Complexes and their Protein Adduct Formation. |
|
dc.type |
Journal Article |
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dc.identifier.doi |
10.1002/anie.202106906 |
|
dc.date.updated |
2021-07-28T11:30:25Z |
|
dc.rights.holder |
Copyright: Wiley-VCH GmbH |
en |
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/34196088 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Journal Article |
|
pubs.elements-id |
858650 |
|
dc.identifier.eissn |
1521-3773 |
|
pubs.number |
anie.202106906 |
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pubs.online-publication-date |
2021-7 |
|