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 | 2022-12-08T06:20:18Z | - |
dc.date.available | 2022-12-08T06:20:18Z | - |
dc.date.created | 2022-12-08 | - |
dc.date.issued | 2022-09 | - |
dc.identifier.issn | 2052-1553 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/114590 | - |
dc.description.abstract | <jats:p>A peptide antibiotic, daptomycin, was repurposed to a multicopper catalyst presenting cooperative rate enhancement in O–O bond formation and activation reactions.</jats:p> 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 (Cun-dap, n = 1-4) in a square planar Cu-N4 geometry, with an axially bound H2O or OH ligand. Cooperative rate enhancement was observed for the O2 activation, H2O2 disproportionation, and O2 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 O2 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. © 2022 The Royal Society of Chemistry. | - |
dc.language | English | - |
dc.publisher | Royal Society of Chemistry | - |
dc.relation.isPartOf | Inorganic Chemistry Frontiers | - |
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.type.rims | ART | - |
dc.identifier.bibliographicCitation | Inorganic Chemistry Frontiers, v.9, no.18, pp.4741 - 4752 | - |
dc.identifier.wosid | 000830665900001 | - |
dc.citation.endPage | 4752 | - |
dc.citation.number | 18 | - |
dc.citation.startPage | 4741 | - |
dc.citation.title | Inorganic Chemistry Frontiers | - |
dc.citation.volume | 9 | - |
dc.contributor.affiliatedAuthor | Choi, Chang Hyuck | - |
dc.identifier.scopusid | 2-s2.0-85135220514 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
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 | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Inorganic & Nuclear | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
library@postech.ac.kr Tel: 054-279-2548
Copyrights © by 2017 Pohang University of Science ad Technology All right reserved.