Abstract
The interaction of Cu 2+ ion with milk xanthine oxidase (XO) has been studied by optical spectroscopy, circular dichroism, ESR and transient kinetic techniques. It is observed that XO forms optically observable complexes with Cu 2+ ion. The pH dependence studies of the formation of Cu 2+–XO complex by optical spectroscopy and circular dichroism show that at least one ionizable group may be responsible for the formation of the complex. The EPR studies show that Cu 2+ ion binds to XO with sulfur and nitrogenous ligands. The transient kinetic study of the interaction of Cu 2+ with XO shows the existence of two Cu 2+ bound XO complexes formed at two different time scales of the interaction, one at ≤5 ms and the other one at around 20 s. The complex formed at longer time scale may be responsible for the inhibition of the enzyme activity.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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