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Deuterohemin-Peptide Enzyme Mimic-Embedded Metal-Organic Frameworks through Biomimetic Mineralization with Efficient ATRP Catalytic Activity Wei Jiang, Xinghuo Wang, Jiawen Chen, Ying Liu, Haobo Han, Yi Ding, Quanshun Li, and Jun Tang ACS Appl. Mater. Interfaces, Just Accepted Manuscript • DOI: 10.1021/acsami.7b09218 • Publication Date (Web): 20 Jul 2017 Downloaded from http://pubs.acs.org on July 21, 2017
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ACS Applied Materials & Interfaces
Deuterohemin-Peptide Enzyme Mimic-Embedded Metal-Organic Frameworks through Biomimetic Mineralization with Efficient ATRP Catalytic Activity
Wei Jiang,† Xinghuo Wang,† Jiawen Chen,‡ Ying Liu,† Haobo Han,‡ Yi Ding,† Quanshun Li,*, ‡ and Jun Tang*, † †
Department of Polymer Science, College of Chemistry, Jilin University, Changchun 130012, China
‡
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China
*
Corresponding author. Tel./Fax: +86-431-88498179. E-mail:
[email protected] (J. Tang);
[email protected] (Q. Li).
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ACS Applied Materials & Interfaces
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ABSTRACT: An enzyme mimic harboring iron porphyrin (DhHP-6) embedded in zeolite imidazolate framework-8 (ZIF-8) was constructed through biomimetic mineralization approach to obtain the composite DhHP-6@ZIF-8. The composite was then used as catalyst in the ATRP of poly(ethylene glycol) methyl ether methacrylate (PEGMA500) in which poly(PEGMA500) could be synthesized with monomer conversion of 76.1% and Mn of 45,900 g/mol, stronger than free DhHP-6 as catalyst. More importantly, it could efficiently overcome the drawbacks of free DhHP-6 and achieve the easy separation of DhHP-6 from the catalytic system and the elimination of iron residues in the synthesized polymer. In addition, it exhibited an enhanced recyclability with monomer conversion of 75.7% after 5 cycles, and favorable stability during ATRP reaction with
