Exploring oxidation-reduction reactions between metal-substituted polyoxometalates and proteins
The redox chemistry between metal-substituted polyoxometalates (POMs) and proteins has been virtually unexplored. Considering a large number of metal-substituted POMs that have been shown to exhibit potent biological activity and reactivity towards biologically relevant substrates, understanding the redox chemistry between POMs and proteins on a molecular level will aid to advance their application in medicinal chemistry and catalysis. Understanding the redox chemistry between metal-substituted POMs and proteins can also be exploited towards their development as catalyst for oxidative cleavage of proteins. In this project we aim to obtain a detailed insight into redox chemistry and molecular interactions between a range of redox-active POMs and proteins. The mechanism of these reactions will be proposed and the possible redox sites in proteins will be identified by applying a range of complementary techniques. We will examine in detail redox chemistry between a range of POMs that are functionalized with redox active metals and a series of proteins. The changes in the protein structures and modification of amino acid side chains will be studied by CD, NMR and UV-Vis spectroscopy and mass spectrometry. The ability of these POMs to oxidize amino acids and promote oxidative cleavage of peptide bonds will be tested by multi-technique approach including MS, IR, NMR spectroscopy measurements.