{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T04:26:46Z","timestamp":1780460806599,"version":"3.54.1"},"reference-count":32,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2023,9,13]],"date-time":"2023-09-13T00:00:00Z","timestamp":1694563200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Universidad de Antioquia for financial","award":["2020000100587"],"award-info":[{"award-number":["2020000100587"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomimetics"],"abstract":"<jats:p>This study focuses on developing and evaluating two novel enantioselective biomimetic models for the active centers of oxidases (ascorbate oxidase and catalase). These models aim to serve as alternatives to enzymes, which often have limited action and a delicate nature. For the ascorbate oxidase (AO) model (compound 1), two enantiomers, S,S(+)cpse and R,R(\u2212)cpse, were combined in a crystalline structure, resulting in a racemic compound. The analysis of their magnetic properties and electrochemical behavior revealed electronic transfer between six metal centers. Compound 1 effectively catalyzed the oxidation of ascorbic to dehydroascorbic acid, showing a 45.5% yield for the racemic form. This was notably higher than the enantiopure compounds synthesized previously and tested in the current report, which exhibited yields of 32% and 28% for the S,S(+)cpse and R,R(-)cpse enantiomers, respectively. This outcome highlights the influence of electronic interactions between metal ions in the racemic compound compared to pure enantiomers. On the other hand, for the catalase model (compound 2), both the compound and its enantiomer displayed polymeric properties and dimeric behavior in the solid and solution states, respectively. Compound 2 proved to be effective in catalyzing the oxidation of hydrogen peroxide to oxygen with a yield of 64.7%. In contrast, its enantiomer (with R,R(-)cpse) achieved only a 27% yield. This further validates the functional nature of the prepared biomimetic models for oxidases. This research underscores the importance of understanding and designing biomimetic models of metalloenzyme active centers for both biological and industrial applications. These models show promising potential as viable alternatives to natural enzymes in various processes.<\/jats:p>","DOI":"10.3390\/biomimetics8050423","type":"journal-article","created":{"date-parts":[[2023,9,12]],"date-time":"2023-09-12T21:41:12Z","timestamp":1694554872000},"page":"423","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Enantioselective Biomimetic Structures Inspired by Oxi-Dase-Type Metalloenzymes, Utilizing Polynuclear Compounds Containing Copper (II) and Manganese (II) Ions as Building Blocks"],"prefix":"10.3390","volume":"8","author":[{"given":"Didier","family":"G\u00f3mez","sequence":"first","affiliation":[{"name":"Facultad de Tecnolog\u00edas, Universidad Tecnol\u00f3gica de Pereira, Pereira 660003, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge","family":"Acosta","sequence":"additional","affiliation":[{"name":"Facultad de Tecnolog\u00edas, Universidad Tecnol\u00f3gica de Pereira, Pereira 660003, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Horacio","family":"L\u00f3pez-Sandoval","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica Inorg\u00e1nica, Facultad de Qu\u00edmica, Universidad Nacional Aut\u00f3noma de M\u00e9xico, C.U., Coyoac\u00e1n, M\u00e9xico City 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4583-9849","authenticated-orcid":false,"given":"Ricardo A.","family":"Torres-Palma","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n en Remediaci\u00f3n Ambiental y Biocat\u00e1lisis (GIRAB), Instituto de Qu\u00edmica, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia UdeA, Calle 70 No. 52-21, Medell\u00edn 50010, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1399-7922","authenticated-orcid":false,"given":"Yenny","family":"\u00c1vila-Torres","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n en Remediaci\u00f3n Ambiental y Biocat\u00e1lisis (GIRAB), Instituto de Qu\u00edmica, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia UdeA, Calle 70 No. 52-21, Medell\u00edn 50010, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,9,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1126\/science.1085515","article-title":"A Perspective on Enzyme Catalysis","volume":"301","author":"Benkovic","year":"2003","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1016\/j.biotechadv.2015.02.014","article-title":"Industrial applications of enzyme biocatalysis: Current status and future aspects","volume":"33","author":"Choi","year":"2015","journal-title":"Biotechnol. 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