期刊
JOURNAL OF MOLECULAR STRUCTURE
卷 1244, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.molstruc.2021.131276
关键词
Mn(II) complex; Isoniazid; Crystal structure; Weak ferromagnetic; Catalase; Interaction
资金
- University of Zabol [IR-UOZ-GR-8288]
- Czech Science Foundation [1810504S]
- Czech Nano Lab Research Infrastructure
- MEYS CR [LM2018110]
A new Mn(II) complex based on oxalato and isoniazid has been synthesized and characterized. The complex exhibited weak ferromagnetic properties and interacted with bovine liver catalase, inhibiting its catalytic activity. The interaction process was found to be spontaneous, exothermic, and driven by Van der Waals and hydrogen bond forces.
A new Mn(II) complex based on oxalato (ox(2-)) and isoniazid (INH), formulated as [Mn(mu-ox)(mu-NIH (N,O)) (mu-NIH (N)Cl](n) (1) has been synthesized under sonochemical irradiation. The molecular structure of complex 1 was studied by elemental analysis, Fourier transform infrared spectroscopy (FT-IR), thermogravimetric analysis (TGA), differential thermal analysis (DTA), vibrating sample magnetometer (VSM), and single-crystal X-ray diffraction (SC-XRD). This complex belongs to a monoclinic system with space group P2(1)/c. X-ray crystallography data revealed Mn(II), adopts a distorted octahedral geometry formed by two nitrogen atoms, three oxygen atoms, and one chloride anion. The results of VSM revealed that in the applied magnetic field up to 15,000 Oe, complex 1 is a weak ferromagnet. The interaction of complex 1 with bovine liver catalase (BLC) was investigated by spectroscopic methods. The enzymatic function of BLC decreased to 45.6% when the concentration of the complex was 6.0 x 10(-6) M. Fluorescence results revealed that the combination of BLC with the complex is subjected to static quenching mechanism (K-b = 1.73 and 0.38 x 10(5) M-1 at 300 and 310 K, respectively). The interaction process was spontaneous, exothermic, and enthalpy-driven, with a major role of Van der Waals and hydrogen bond forces. UV-Vis, 3D, and synchronous fluorescence measurements indicated the changes in the microenvironment residues of BLC in the presence of complex 1. In conclusion, the above complex can interact with catalase and so inhibit its catalytic activity for the decomposition of hydrogen peroxide. (C) 2021 Elsevier B.V. All rights reserved.
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