Publications
Detailed Information
Repurposing a peptide antibiotic as a catalyst: a multicopper-daptomycin complex as a cooperative O-O bond formation and activation catalyst
Cited 0 time in
Web of Science
Cited 0 time in Scopus
- Authors
- Issue Date
- 2022-09
- Publisher
- Royal Society of Chemistry
- Citation
- Inorganic Chemistry Frontiers, Vol.9 No.18, pp.4741-4752
- Abstract
- In naturally occurring metalloenzymes, cooperative multimetallic sites activate, cleave, and form dioxygen bonds. Thus, molecular scaffolds providing multimetallic sites are increasingly being exploited to develop cooperative redox catalysts. Herein, we report a multicopper complex based on a peptide antibiotic, daptomycin (dap), which mediates O-O bond formation and activation reactions. In alkaline media, UV-vis and electron paramagnetic resonance (EPR) spectroscopy showed that dap stabilized up to four Cu(ii) ions (Cu-n-dap, n = 1-4) in a square planar Cu-N-4 geometry, with an axially bound H2O or OH ligand. Cooperative rate enhancement was observed for the O-2 activation, H2O2 disproportionation, and O-2 evolution reactions, only in the presence of the multimetallic Cu complex. In situ Raman spectroscopy was used to study the intermediate species involved in the electrochemical O-2 evolution reaction and understand the catalytic mechanism behind the O-O bond formation. The observed Cu-O species related to the Cu2O2 core suggested a possible radical coupling pathway for the O-O bond formation. This study provides a strategy to repurpose natural calcium-binding peptide antibiotics as ligands, to create multimetallic sites for cooperative catalysis.
- ISSN
- 2052-1553
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.