Carbene in Cupredoxin Protein Scaffolds: Replacement of a Histidine Ligand in the Active Site Substantially Alters Copper Redox Properties
| Autor: | Matteo Planchestainer, Nathalie Segaud, Muralidharan Shanmugam, Jonathan McMaster, Francesca Paradisi, Martin Albrecht |
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| Rok vydání: | 2018 |
| Předmět: |
Copper protein
Stereochemistry Homogeneous catalysis Ligands 010402 general chemistry 01 natural sciences Redox Catalysis metalloenyzme histidine bonding mode N-heterocyclic carbene electron transfer processes chemistry.chemical_compound Azurin Heterocyclic Compounds Manchester Institute of Biotechnology Catalytic Domain Cupredoxin Histidine N-Heterocylic Carbene biology 010405 organic chemistry Ligand Electron Spin Resonance Spectroscopy Active site General Medicine Electrochemical Techniques General Chemistry ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology 0104 chemical sciences 3. Good health chemistry Spectrophotometry Mutagenesis Site-Directed biology.protein EPR Methane Oxidation-Reduction Carbene Copper |
| Zdroj: | Angewandte Chemie International Edition Planchestainer, M, Segaud, N, Shanmugam, M, Mcmaster, J, Paradisi, F & Albrecht, M 2018, ' Carbene in Cupredoxin Protein Scaffolds: Replacement of a Histidine Ligand in the Active Site Substantially Alters Copper Redox Properties ', Angewandte Chemie International Edition, vol. 57, no. 33, pp. 10677-10682 . https://doi.org/10.1002/anie.v57.33 |
| ISSN: | 1433-7851 1521-3773 |
| DOI: | 10.1002/anie.201807168 |
| Popis: | N-heterocyclic carbene (NHC) ligands have hada major impact in homogeneous catalysis, however, theirpotential role in biological systems is essentially unexplored.We replaced a copper-coordinating histidine (His) in the activesite of the redox enzyme azurin with exogenous dimethylimidazolylidene. This NHC rapidly restores the type-1 Cucenter, with spectroscopic properties (EPR, UV/Vis) that areidentical to those from N-coordination of the His in the wildtype. However, the introduction of the NHC markedly altersthe redox potential of the metal, which is a key functionality ofthis blue copper protein. These results suggest that C-bondingfor histidine is plausible and a potentially relevant bondingmode of redox-active metalloenzymes in their (transient) activestates. |
| Databáze: | OpenAIRE |
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