Sau, Apurba Kumar ; Mondal, Madhu Sudan ; Mitra, Samaresh (2001) Interaction of Cu2+ ion with milk xanthine oxidase Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1544 (1-2). pp. 89-95. ISSN 0167-4838
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S01674...
Related URL: http://dx.doi.org/10.1016/S0167-4838(00)00207-7
Abstract
The interaction of Cu2+ 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 Cu2+ ion. The pH dependence studies of the formation of Cu2+-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 Cu2+ ion binds to XO with sulfur and nitrogenous ligands. The transient kinetic study of the interaction of Cu2+ with XO shows the existence of two Cu2+ 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.
Item Type: | Article |
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Source: | Copyright of this article belongs to Elsevier Science. |
Keywords: | Xanthine Oxidase; Copper Ion; Circular Dichroism; Stopped Flow Kinetics |
ID Code: | 20098 |
Deposited On: | 20 Nov 2010 15:01 |
Last Modified: | 03 Mar 2011 07:52 |
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