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Kholdeeva, O., Skobelev, A., Kovalenko I.Y., Konstantin, A., et al. (2013) Solvent-Free Al-lylic Oxidation of Alkenes with O-2 Mediated by Fe- and Cr-MIL-101. Journal of Catalysis, 298, 61-69. https://doi.org/10.1016/j.jcat.2012.11.003

has been cited by the following article:

• TITLE: MOFzyme: Enzyme Mimics of Fe/Fe-MIL-101

  AUTHORS: Lingli Li, Daomei Chen, Bin Li, Dongqi Yang, Jingchen Zhao, Danhua Ma, Liang Jiang, Yepeng Yang, Yizhou Li, Jiaqiang Wang

  KEYWORDS: Metal-Organic Frameworks (MOFs), Fe-MIL-101, 5% Fe/Fe-MIL-101, Peroxidase Mimetics

  JOURNAL NAME: Journal of Biosciences and Medicines, Vol.7 No.5, May 31, 2019

  ABSTRACT: In this work, metal-organic frameworks (MOFs) Fe-MIL-101 was synthesized by hydrothermal method, and Fe/Fe-MIL-101 with different loadings was prepared. The crystal structure of the Fe/Fe-MIL-101 sample was characterized by scanning electron microscopy (SEM), X-ray diffraction (XRD) and specific surface area measurement (BET). Fe/Fe-MIL-101 was found to posses an intrinsic enzyme mimicking activity similar to that found in natural horse-radish peroxidase (HRP). The Michaelis constant (Km) of 5% Fe/Fe-MIL-101 with ABTS as the substrate is about 10-fold smaller than Fe-MIL-101 and about 3-fold smaller than HRP, and about 108 times less than that of CuO NPs (Km = 10.28 mM), indicating a much higher affinity for ABTS than HRP and most of the peroxidase mimetics.