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Why Does Enzyme Not Leach from Metal–Organic Frameworks (MOFs)? Unveiling the Interactions between an Enzyme Molecule and a MOF
The strong interactions between microperoxidase (MP-11) and Tb-mesoMOF were identified via Raman spectroscopic studies, which revealed that MP-11 molecules interact with the framework of Tb-mesoMOF through π···π interactions between the heme of MP-11 and the conjugated triazine and benzene rings in...
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Published in: | Inorganic chemistry 2014-10, Vol.53 (19), p.10006-10008 |
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creator | Chen, Yao Han, Sungyub Li, Xiao Zhang, Zhenjie Ma, Shengqian |
description | The strong interactions between microperoxidase (MP-11) and Tb-mesoMOF were identified via Raman spectroscopic studies, which revealed that MP-11 molecules interact with the framework of Tb-mesoMOF through π···π interactions between the heme of MP-11 and the conjugated triazine and benzene rings in the organic ligand of Tb-mesoMOF. The strong interactions facilitate the retention of MP-11 molecules within the metal–organic framework (MOF) pores, which is in striking contrast with the severe leaching of MP-11 from MCM-41 due to the lack of specific interactions between enzyme molecules and the mesoporous silica material. |
doi_str_mv | 10.1021/ic501062r |
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subjects | Models, Molecular Molecular Structure Organometallic Compounds - chemistry Organometallic Compounds - metabolism Peroxidases - chemistry Peroxidases - metabolism Terbium - chemistry Terbium - metabolism |
title | Why Does Enzyme Not Leach from Metal–Organic Frameworks (MOFs)? Unveiling the Interactions between an Enzyme Molecule and a MOF |
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