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Multicopper Laccase Mimicking Nanozymes with Nucleotides as Ligands

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dc.contributor.authorLiang, Hao
dc.contributor.authorLin, Feifei
dc.contributor.authorZhang, Zijie
dc.contributor.authorLiu, Biwu
dc.contributor.authorJiang, Shuhui
dc.contributor.authorYuan, Qipeng
dc.contributor.authorLiu, Juewen
dc.date.accessioned2017-04-28T16:11:53Z
dc.date.available2017-04-28T16:11:53Z
dc.date.issued2017-01-18
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Applied Materials & Interfaces, © 2017 American Chemical Society after peer review and technical editing by publisher. To access the final edited and published work see Liang, H., Lin, F., Zhang, Z., Liu, B., Jiang, S., Yuan, Q., & Liu, J. (2017). Multicopper Laccase Mimicking Nanozymes with Nucleotides as Ligands. Acs Applied Materials & Interfaces, 9(2), 1352–1360. https://doi.org/10.1021/acsami.6b15124en
dc.description.abstractUsing nanomaterials to achieve functional enzyme mimics (nanozymes) is attractive for both applied and fundamental research. Laccases are multicopper oxidases highly important for biotechnology and environmental remediation. In this work, we report an exceptionally simple yet functional laccase mimic based on guanosine monophosphate (GMP) coordinated copper. It forms an amorphous metal organic framework (MOP) material. The ratio of copper and GMP is 3:4 as determined by isothermal titration calorimetry. It has excellent laccase-like activity and converts a diverse range of phenol containing substrates such as hydroquinone, naphthol, catechol and epinephrine. Comparative work shows that the activity is originated from guanosine coordination instead of phosphate binding in GMP. Cu2+ is required and cannot be substituted by other metal ions. At the same mass concentration, the Cu/GMP nanozyme has a higher V-max and similar K-m compared to the protein laccase. To achieve the same catalytic efficiency, the cost of the Gu/GMP is similar to 2400-fold lower than that of laccase. The Cu/GMP is much more stable at extreme pH, high salt, high temperature and for long-term storage. This is one of the first laccase-mimicking nanozymes, which will find important applications in analytical chemistry, environmental protection, and biotechnology.en
dc.description.sponsorshipBeijing Natural Science Foundation [2162030]; Fundamental Research Funds for the Central Universities [YS1407]; China Scholarship Council; 111 project; Natural Sciences and Engineering Research Council of Canada (NSERC)en
dc.identifier.urihttp://dx.doi.org/10.1021/acsami.6b15124
dc.identifier.urihttp://hdl.handle.net/10012/11781
dc.language.isoenen
dc.publisherAmerican Chemical Societyen
dc.subjectMetal-Organic Frameworksen
dc.subjectBiocoordination Polymersen
dc.subjectEnzymesen
dc.subjectNanoparticlesen
dc.subjectComplexesen
dc.subjectMoleculesen
dc.subjectOxidationen
dc.subjectMechanismen
dc.subjectChiralityen
dc.subjectGlucoseen
dc.titleMulticopper Laccase Mimicking Nanozymes with Nucleotides as Ligandsen
dc.typeArticleen
dcterms.bibliographicCitationLiang, H., Lin, F., Zhang, Z., Liu, B., Jiang, S., Yuan, Q., & Liu, J. (2017). Multicopper Laccase Mimicking Nanozymes with Nucleotides as Ligands. Acs Applied Materials & Interfaces, 9(2), 1352–1360. https://doi.org/10.1021/acsami.6b15124en
uws.contributor.affiliation1Faculty of Scienceen
uws.contributor.affiliation2Chemistryen
uws.contributor.affiliation3Waterloo Institute for Nanotechnology (WIN)en
uws.peerReviewStatusRevieweden
uws.scholarLevelFacultyen
uws.typeOfResourceTexten

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