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 cooperat...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,dap-tomycin(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(Cun-dap,n=1-4)in a square planar Cu-N_(4)geometry,with an axially bound H_(2)O or OH ligand.Cooperative rate enhancement was observed for the O_(2)activation,H_(2)O_(2)disproportionation,and O_(2)evol-ution 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 under-stand the catalytic mechanism behind the O-O bond formation.The observed Cu-O species related to the Cu_(2)O_(2)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 multime-tallic sites for cooperative catalysis.展开更多
基金supported by the Creative Materials Discovery Program(NRF-2018M3D1A1052659 to J.S.,NRF-2017M3D1A1039378 to C.H.C.,NRF-2017M3D1A1039377 to K.T.N.and NRF-2017M3D1A1039380 to S.H.K.)by the National Research Foundation of Korea(NRF-2021R1A2C2014421 to J.S.)which is funded by the National Research Foundation(NRF)under the Ministry of Science and ICT.
文摘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,dap-tomycin(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(Cun-dap,n=1-4)in a square planar Cu-N_(4)geometry,with an axially bound H_(2)O or OH ligand.Cooperative rate enhancement was observed for the O_(2)activation,H_(2)O_(2)disproportionation,and O_(2)evol-ution 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 under-stand the catalytic mechanism behind the O-O bond formation.The observed Cu-O species related to the Cu_(2)O_(2)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 multime-tallic sites for cooperative catalysis.
