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Investigation of xanthine oxidase. Magnetic circular dichroism studies.

The magnetic circular dichroism and circular dichroism spectra of xanthine oxidase are reported from 200–700 nm. The magnetic circular dichroism spectrum exhibits weak bands at 520 and 375 nm which are assigned to the iron-sulfur and molybdenum chromophores, respectively. The tryptophan chromophore gives a strong positive magnetic circular dichroism band at 292 nm and from the intensity of this band in xanthine oxidase, the presence of a total of 23–24 residues per molecule has been calculated.