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Repurposing a peptide antibiotic as a catalyst: a multicopper-daptomycin complex as a cooperative O-O bond formation and activation catalyst
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Yen Jea | - |
dc.contributor.author | Kim, Haesol | - |
dc.contributor.author | Kim, Yujeong | - |
dc.contributor.author | Cho, Kang Hee | - |
dc.contributor.author | Hong, Sugyeong | - |
dc.contributor.author | Nam, Ki Tae | - |
dc.contributor.author | Kim, Sun Hee | - |
dc.contributor.author | Choi, Chang Hyuck | - |
dc.contributor.author | Seo, Jiwon | - |
dc.date.accessioned | 2022-10-07T01:25:55Z | - |
dc.date.available | 2022-10-07T01:25:55Z | - |
dc.date.created | 2022-09-20 | - |
dc.date.created | 2022-09-20 | - |
dc.date.created | 2022-09-20 | - |
dc.date.created | 2022-09-20 | - |
dc.date.created | 2022-09-20 | - |
dc.date.created | 2022-09-20 | - |
dc.date.issued | 2022-07 | - |
dc.identifier.citation | Inorganic Chemistry Frontiers, Vol.9 No.18, pp.4741-4752 | - |
dc.identifier.issn | 2052-1553 | - |
dc.identifier.uri | https://hdl.handle.net/10371/185565 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.publisher | Royal Society of Chemistry | - |
dc.title | Repurposing a peptide antibiotic as a catalyst: a multicopper-daptomycin complex as a cooperative O-O bond formation and activation catalyst | - |
dc.type | Article | - |
dc.identifier.doi | 10.1039/d2qi01440h | - |
dc.citation.journaltitle | Inorganic Chemistry Frontiers | - |
dc.identifier.wosid | 000830665900001 | - |
dc.identifier.scopusid | 2-s2.0-85135220514 | - |
dc.citation.endpage | 4752 | - |
dc.citation.number | 18 | - |
dc.citation.startpage | 4741 | - |
dc.citation.volume | 9 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Nam, Ki Tae | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | ELECTROCATALYTIC WATER OXIDATION | - |
dc.subject.keywordPlus | CYTOCHROME-C-OXIDASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | MOLECULAR-OXYGEN | - |
dc.subject.keywordPlus | METAL-BINDING | - |
dc.subject.keywordPlus | ASCORBIC-ACID | - |
dc.subject.keywordPlus | COPPER | - |
dc.subject.keywordPlus | COORDINATION | - |
dc.subject.keywordPlus | REDUCTION | - |
dc.subject.keywordPlus | CHEMISTRY | - |
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