Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties
N-heterocyclic carbene (NHC) ligands have had a major impact in homogeneous catalysis, however, their potential role in biological systems is essentially unexplored. Here we replaced a copper-coordinating histidine (His) in the active site of azurin with exogenous dimethyl-imidazolylidene; this NHC...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Published: |
Wiley-VCH Verlag
2018
|
| Subjects: | |
| Online Access: | https://eprints.nottingham.ac.uk/52943/ |
| _version_ | 1848798844084551680 |
|---|---|
| author | Planchestainer, Matteo Segaud, Nathalie Shanmugam, Muralidharan McMaster, Jonathan Paradisi, Francesca Albrecht, Martin |
| author_facet | Planchestainer, Matteo Segaud, Nathalie Shanmugam, Muralidharan McMaster, Jonathan Paradisi, Francesca Albrecht, Martin |
| author_sort | Planchestainer, Matteo |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | N-heterocyclic carbene (NHC) ligands have had a major impact in homogeneous catalysis, however, their potential role in biological systems is essentially unexplored. Here we replaced a copper-coordinating histidine (His) in the active site of azurin with exogenous dimethyl-imidazolylidene; this NHC rapidly restores the type-1 Cu center with spectroscopic properties (EPR, UV-vis) that are identical to those from N-coordination of the His in the wild type. However, the introduction of the NHC markedly alters the redox potential of the metal, key functionality of this blue copper protein. These results suggest that C-bonding for histidine is plausible and a potentially relevant bonding mode of redox-active metalloenzymes in their (transient) active states. |
| first_indexed | 2025-11-14T20:26:13Z |
| format | Article |
| id | nottingham-52943 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T20:26:13Z |
| publishDate | 2018 |
| publisher | Wiley-VCH Verlag |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-529432020-05-04T19:42:36Z https://eprints.nottingham.ac.uk/52943/ Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties Planchestainer, Matteo Segaud, Nathalie Shanmugam, Muralidharan McMaster, Jonathan Paradisi, Francesca Albrecht, Martin N-heterocyclic carbene (NHC) ligands have had a major impact in homogeneous catalysis, however, their potential role in biological systems is essentially unexplored. Here we replaced a copper-coordinating histidine (His) in the active site of azurin with exogenous dimethyl-imidazolylidene; this NHC rapidly restores the type-1 Cu center with spectroscopic properties (EPR, UV-vis) that are identical to those from N-coordination of the His in the wild type. However, the introduction of the NHC markedly alters the redox potential of the metal, key functionality of this blue copper protein. These results suggest that C-bonding for histidine is plausible and a potentially relevant bonding mode of redox-active metalloenzymes in their (transient) active states. Wiley-VCH Verlag 2018-08-13 Article PeerReviewed Planchestainer, Matteo, Segaud, Nathalie, Shanmugam, Muralidharan, McMaster, Jonathan, Paradisi, Francesca and Albrecht, Martin (2018) Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties. Angewandte Chemie International Edition, 57 (33). pp. 10677-10682. ISSN 1521-3773 metalloenyzme histidine bonding mode N-heterocyclic carbene electron transfer processes https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201807168 doi:10.1002/anie.201807168 doi:10.1002/anie.201807168 |
| spellingShingle | metalloenyzme histidine bonding mode N-heterocyclic carbene electron transfer processes Planchestainer, Matteo Segaud, Nathalie Shanmugam, Muralidharan McMaster, Jonathan Paradisi, Francesca Albrecht, Martin Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title | Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title_full | Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title_fullStr | Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title_full_unstemmed | Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title_short | Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| title_sort | carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties |
| topic | metalloenyzme histidine bonding mode N-heterocyclic carbene electron transfer processes |
| url | https://eprints.nottingham.ac.uk/52943/ https://eprints.nottingham.ac.uk/52943/ https://eprints.nottingham.ac.uk/52943/ |