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Three new Strandberg-type phenylphosphomolybdate supports for immobilizing horseradish peroxidase and their catalytic oxidation performances.

A new interesting article has been published in Dalton Trans. 2018 Oct 9;47(39):14060-14069. doi: 10.1039/c8dt03102a. and titled:

Three new Strandberg-type phenylphosphomolybdate supports for immobilizing horseradish peroxidase and their catalytic oxidation performances.

Authors of this article are:
Feng SL 1, Lu Y , Zhang YX , Su F , Sang XJ , Zhang LC , You WS , Zhu ZM .

A summary of the article is shown below:
Three organic-inorganic hybrids containing Strandberg-type phenylphosphomolybdate anion [(C6H5PO3)2Mo5O15]4- with phenylphosphonate (PhP) centers, transition metal (TM) ions and 2,2′-biimidazole (H2biim) ligand, formulated as [(TM(H2biim)2)2(C6H5PO3)2Mo5O15]·H2O (TM = Co and Cu, abbreviated as Co-(PhP)2Mo5 and Cu-(PhP)2Mo5, respectively) and ([Ni(H2biim)3])2[(C6H5PO3)2Mo5O15]·2H2O (abbreviated as Ni-(PhP)2Mo5), were self-assembled by simple hydrothermal methods and were systematically characterized through single-crystal X-ray diffraction and other physicochemical and spectroscopic methods, which demonstrated that TM-H2biim complexes were firstly introduced into Strandberg-type organophosphomolybdate skeletons. Selecting the oxidation of cyclohexanol to cyclohexanone as a model reaction, using H2O2 as an oxidant, the catalytic oxidation activities of the Strandberg-type compounds were firstly evaluated. More importantly, these TM-(PhP)2Mo5 (TM = Co, Cu, Ni) compounds were employed to immobilize horseradish peroxidase (HRP), and showed high adsorption capacities for HRP. Laser scanning confocal microscope images showed that HRP adsorbed on the surfaces of the TM-(PhP)2Mo5 supports. Application of immobilized enzyme HRP/TM-(PhP)2Mo5 for the detection of H2O2 is also discussed.

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