Zinc and Oxo-Vanadium Complexes upon Binding to Phosphatase Enzymes: Structure, Electronics and Implications

Oxovanadium and zinc complexes are reported as insulin-mimetics. They inhibit several proteins including enzymes which belong to the same class of membrane sensitive phosphatases, similar in terms of general architecture and biochemistry of the active site. Borrowing from this summary, we explore the structural and electronic properties of representative oxovanadium and zinc complexes as computed in isolation and upon binding to PTEN and PTP1B phosphatases. Using crystallographic data and quantum chemistry calculations, we investigate how bonding nature and structural flexibility of the studied inhibitors affects efficiency of their binding to the active sites of the enzymes: albeit different, the two active sites represent evolutionary variant choices of the same type of biochemistry of phosphatases. As a result of our studies, we address optical responses which can be suitable for diagnostics and discuss engineering of AI assisted protein embedding to alter electronic states of metal centres which may be beneficial for biomedical and quantum information applications within the bio-spintronics of tomorrow.