Madhu Sudan Mondal
Articles written in Journal of Chemical Sciences
Volume 106 Issue 1 February 1994 pp 29-35 Inorganic and Analytical
Inhibition of oxidoreductase activity of xanthine oxidase by Cu2+ and Hg2+ ions
Madhu Sudan Mondal Digambar V Behere Samaresh Mitra
Xanthine oxidase has been isolated in good yield and pure form. Inhibition of the enzyme by Cu2+ and Hg2+ ions has been studied. The nature and extent of the inhibition have been determined.
Volume 106 Issue 3 June 1994 pp 767-767
Interaction of metal ions on the transient reductive half reaction of xanthine oxidase
Volume 111 Issue 3 June 1999 pp 501-508 Modern Trends In Inorganic Chemistry
Altered redox affinity of xanthine oxidase active sites by copper(II) ions
Madhu Sudan Mondal Samaresh Mitra
The interaction of Cu2+ ion with the redox centres of xanthine oxidase (XO) has been investigated using optical difference spectroscopic measurements. Anaerobic enzyme-reduction experiments using controlled and excess substrates (xanthine and NADH) have been performed to investigate the perturbation of XO active sites in the presence of Cu2+ ions. The results indicate an overall alteration in the redox affinities (i.e. affinity to accept electrons) of the active sites of XO by Cu2+ ion.
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