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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

Authors

Matteo Planchestainer

Nathalie Segaud

Muralidharan Shanmugam

Martin Albrecht



Abstract

© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim N-heterocyclic carbene (NHC) ligands have had a major impact in homogeneous catalysis, however, their potential role in biological systems is essentially unexplored. We replaced a copper-coordinating histidine (His) in the active site of the redox enzyme 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, which is a 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.

Citation

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, 57(33), 10677-10682. https://doi.org/10.1002/anie.201807168

Journal Article Type Article
Acceptance Date Jun 27, 2018
Online Publication Date Jun 27, 2018
Publication Date Aug 13, 2018
Deposit Date Jul 13, 2018
Publicly Available Date Jun 28, 2019
Journal Angewandte Chemie International Edition
Print ISSN 1433-7851
Electronic ISSN 1521-3773
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 57
Issue 33
Pages 10677-10682
DOI https://doi.org/10.1002/anie.201807168
Keywords metalloenyzme histidine bonding mode N-heterocyclic carbene electron transfer processes
Public URL http://eprints.nottingham.ac.uk/id/eprint/52943
Publisher URL https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201807168
Copyright Statement Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf

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Copyright Statement
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf





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